IndraLab

Statements



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"Importantly, expression of WT, but not mutant USP27X, prevented the proliferation defects caused by depletion of endogenous USP27X (XREF_FIG)."

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"Importantly, expression of WT, but not mutant USP27X, prevented the proliferation defects caused by depletion of endogenous USP27X."

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"Furthermore, USP27 or SETD3 knockdown inhibits cell proliferation, cell migration and tumorigenesis, while overexpression of SETD3 in USP27-deficient HCC cells could restore cell viability."

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"Knockdown of USP27 by short hairpin RNA (shRNA) accelerated the degradation of SETD3 and blocked cell proliferation."

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"To determine how USP27X promotes cancer cell proliferation, we first performed immunoblots comparing the expression of several cell signaling molecules."

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"The observation that USP27 promotes cell cycle progression and cell proliferation prompted us to imagine that depletion of USP27 expression might suppress tumor progression."

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"Herein, we demonstrate that USP27 regulates Cyclin E abundance to accelerate cell cycle progression, cell proliferation, and tumor cell growth as well."

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"These results suggest that USP27X is required to support cancer cell proliferation as opposed to regulating cell death."

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"Furthermore, cell proliferation was also remarkably reduced in the combination of USP27 knockdown and 5-FU treatment, whereas overexpression of USP27 or addition of Cyclin E in USP27 knockdown cells could raise cell proliferation."

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"Expression of WT-USP27X on its own led to slightly increased proliferation, whereas expression of the C285S mutant led to slightly reduced proliferation."

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"Importantly, expression of WT, but not mutant USP27X, prevented the proliferation defects caused by depletion of endogenous USP27X."

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"Importantly, expression of WT, but not mutant USP27X, prevented the proliferation defects caused by depletion of endogenous USP27X (XREF_FIG)."
USP27X affects CCND1
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USP27X decreases the amount of CCND1.
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USP27X decreases the amount of CCND1. 5 / 5
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"These experiments revealed that indeed, overexpression of WT but not catalytically inactive USP27X drastically reduces the level of CCND1 ubiquitination (Fig. 3J, compare lanes 7, 8, and 9)."

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"These data indicated that, indeed, loss of USP27X, which reduces the levels of CCND1, leads to reduction of the CCND1-CDK4/6 complexes and, therefore, loss of Rb1 phosphorylation."

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"Ablation of USP27X in xenograft tumors reduces CCND1 levels and impairs growth.."

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"Moreover, ablation of USP27X drastically reduces CCND1 levels in these cells and arrests their growth in an Rb1-dependent manner."

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"Hence, we next tested whether USP27X ablation, which reduces CCND1 levels, would resensitize HER2 therapy resistant cells to targeted therapy."
USP27X increases the amount of CCND1.
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USP27X increases the amount of CCND1. 4 / 4
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"As expected, USP27X depletion substantially reduced both CCND1 levels and Rb1 phosphorylation in these cells (Fig. 5E, compare lane 1 to 2)."

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"These data indicated that, indeed, loss of USP27X, which reduces the levels of CCND1, leads to reduction of the CCND1-CDK4/6 complexes and, therefore, loss of Rb1 phosphorylation."

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"The expression of exogenous WT USP27X only increased CCND1 levels slightly above the levels in non-depleted, vector only cells (Fig. 3G, lane1)."

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"These experiments demonstrated that the expression of WT but not catalytically inactive USP27X can restore the levels of CCND1 in depleted cells (Fig. 3G, compare lanes 2, 3, and 4)."
USP27X deubiquitinates CCND1.
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USP27X deubiquitinates CCND1. 4 / 4
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"As shown in Figure 3D, USP27X depletion led to a substantial increase in CCND1 ubiquitination (Fig. 3D compare lane 9 to 10)."

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"These experiments revealed that indeed, overexpression of WT but not catalytically inactive USP27X drastically reduces the level of CCND1 ubiquitination (Fig. 3J, compare lanes 7, 8, and 9)."

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"Overexpression of USP27X reduces CCND1 ubiquitination and stabilizes the protein, while USP27X ablation reduces CCND1 stability."

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"To test if USP27X can deubiquitinate CCND1 in cells, we overexpressed WT or CS USP27X in JIMT-1 cells, treated with MG132 to block proteasomal degradation, and monitored CCND1 ubiquitination after protein immunoprecipitation (Fig. 3J)."
USP27X ubiquitinates CCND1.
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USP27X leads to the ubiquitination of CCND1. 1 / 1
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"Next, we sought to test whether USP27X ablation leads to increased CCND1 ubiquitination."
USP27X phosphorylates CCND1.
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USP27X leads to the phosphorylation of CCND1. 1 / 1
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"As expected, USP27X depletion substantially reduced both CCND1 levels and Rb1 phosphorylation in these cells (Fig. 5E, compare lane 1 to 2)."
USP27X inhibits CCND1.
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USP27X inhibits CCND1. 1 / 1
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"As expected, USP27X ablation accelerated the degradation of CCND1 (half-life of ~15 minutes in shProLuc vs. ~8 minutes in shUSP27X), confirming that CCND1 protein stability is compromised upon USP27X loss (Fig. 3E, F)."
USP27X binds CCND1.
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"USP27X binds to and stabilizes CCND1 in a catalytically-dependent manner by negatively regulating its ubiquitination."
USP27X activates CCND1.
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USP27X activates CCND1. 1 / 1
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"As expected, expression of WT USP27X prolonged CCND1 stability (half-life not detected) while CS USP27X accelerated CCND1 degradation (~18 minutes vs. 15 minutes) (Fig. 3H, compare lanes 3 and 4 to 7, 8,10, 11; Fig 3I)."
USP27X affects BCL2L11
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USP27X deubiquitinates BCL2L11.
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USP27X deubiquitinates BCL2L11. 5 / 5
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"Moreover, USP27 deubiquitinates and stabilizes the BH3-only protein Bim, subsequently enhancing apoptosis [14]."

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"Thus, Usp27x can trigger via its proteolytic activity the deubiquitination of Bim and enhance its levels, counteracting the anti-apoptotic effects of ERK activity, and therefore acts as a tumour suppressor."

"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."

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"For example, Weber et al. found that wild-type USP27 can reduce the levels of Bim ubiquitination and stabilize Bim in response to the Raf‐ERK‐degradation signal [14]."

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"Overexpression of USP27x combined with ERK1/2 activation to promote the deubiquitylation and stabilisation of BIM and increase caspase‐dependent apoptosis."
Modified USP27X leads to the deubiquitination of BCL2L11. 1 / 1
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"Overexpression of Usp27x reduces ERK dependent Bim ubiquitination, stabilizes phosphorylated Bim, and induces apoptosis in PMA stimulated cells, as well as in tumour cells with a constitutively active Raf and ERK pathway."
USP27X binds BCL2L11.
3 | 2 1
3 | 2

No evidence text available

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"USP27x, acting as a tumor suppressor, could bind to Bim upon its anti-apoptotic ERK dependent phosphorylation and counteract the following proteasomal degradation via its deubiquitinase activity."

No evidence text available

No evidence text available

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"Furthermore, like βTrCP1/2, the binding of USP27x to BIM was dependent upon ERK1/2 activation."
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sparser
"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."
USP27X inhibits BCL2L11.
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"Cathepsin K inhibition induced mitochondrial ROS enhances sensitivity of cancer cells to anti-cancer drugs through USP27x mediated Bim protein stabilization."

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"Loss of endogenous Usp27x enhances the Bim degrading activity of oncogenic Raf."

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"USP27x DUB antagonizes the Raf-ERK Bim degradation pathway thus stabilizing Bim expression."
USP27X decreases the amount of BCL2L11.
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USP27X decreases the amount of BCL2L11. 1 / 1
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"For example, Weber et al. found that wild-type USP27 can reduce the levels of Bim ubiquitination and stabilize Bim in response to the Raf‐ERK‐degradation signal [14]."
USP27X affects SETD3
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USP27X deubiquitinates SETD3.
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USP27X deubiquitinates SETD3. 5 / 5
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"USP27 was able to deubiquitinate and stabilize SETD3."

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"We found that SETD3 was deubiquitinated and stabilized by USP27."

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"USP27 inhibits the K48-linkage poly-ubiquitination of SETD3."

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"Similar results were obtained in the analysis of SETD3.Based on our results, we concluded that SETD3 is deubiquitinated by USP27 and its protein level is positively regulated by and correlated with USP27 expression."

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"Since USP27 could deubiquitinate and stabilize SETD3, it might promote cell proliferation and migration by regulating SETD3 protein levels."
USP27X-C87A deubiquitinates SETD3. 1 / 1
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"As seen in Fig. 2C, an enzyme-inactive mutant of USP27 (C87A) failed to abolish the ubiquitination of SETD3 protein compared with the wild-type (WT) USP27, implying that the DUB activity is required for USP27 to remove ubiquitin from SETD3."
USP27X activates SETD3.
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USP27X activates SETD3. 4 / 4
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"Knockdown of USP27 by short hairpin RNA (shRNA) accelerated the degradation of SETD3 and blocked cell proliferation."

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"Since upregulation of SETD3 can promote liver tumorigenesis and cancer progression [12], it is possible that USP27 can also enhance metastatic phenotype by stabilizing SETD3."

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"Inhibition of USP27 expression impairs the pro-migratory ability of SETD3."

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"In conclusion, our data suggested that USP27 could positively regulate SETD3 protein stability."
USP27X increases the amount of SETD3.
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USP27X increases the amount of SETD3. 2 / 2
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"As shown in Fig. 3A and B, SETD3 protein expression is significantly upregulated by cotransfection of USP27 and the half-life of the SETD3 protein is dramatically extended by USP27."

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"Furthermore, ectopic expression of USP27 upregulated endogenous SETD3 protein levels (Fig. 3C and D)."
USP27X inhibits SETD3.
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USP27X inhibits SETD3. 1 / 1
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"Finally, no obvious change in the mRNA expression levels of SETD3 was observed in the Hep3B cells showing USP27 overexpression (Fig. 3K), suggesting that the regulation of SETD3 protein degradation by USP27 might occur at the post-transcriptional level."
USP27X binds SETD3.
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"To further confirm that the interaction between SETD3 and USP27 was specific, we transfected them alone or together into 293 T cells and evaluated their interaction by immunoprecipitation and western blot."
USP27X affects Cyclin_E
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USP27X activates Cyclin_E.
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"USP27 mediated Cyclin E stabilization drives cell cycle progression and hepatocellular tumorigenesis."

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"XREF_FIG, MG132 (proteasome inhibitor) treatment could rescue the USP27 knockdown mediated degradation of Cyclin E protein."

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"Our discovery that USP27 mediated Cyclin E stabilization implied that USP27 might modulate cell cycle and cell proliferation through Cyclin E regulation."

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"XREF_FIG, catalytically inactive USP27/CA mutant failed to protect Cyclin E from degradation, implying that the DUB activity is required for USP27 mediated Cyclin E stabilization."

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"USP27 mediated Cyclin E stabilization is involved in tumorigenesis, suggesting that targeting USP27 may represent a new therapeutic strategy to treat cancers with aberrant overexpression of Cyclin E protein."

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"Finally, we determined whether USP27 mediated Cyclin E stability is through proteasome."
USP27X binds Cyclin_E.
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"To prevent this degradation, USP27 interacts with and deubiquitinates cyclin E [66]."

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"The observation that USP27 interacts with and deubiquitinates Cyclin E led us to think that USP27 might involve in cell cycle progression by regulating Cyclin E stability."

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"In addition, we examined whether endogenous Cyclin E interacts with USP27 in the Hep3B cells."

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"To further confirm that the interaction between Cyclin E and USP27 was specific, we transfected them alone or together into HEK293T cells and evaluated their interaction by immunoprecipitation and WB."
USP27X deubiquitinates Cyclin_E.
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USP27X deubiquitinates Cyclin_E. 3 / 3
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"The observation that USP27 interacts with and deubiquitinates Cyclin E led us to think that USP27 might involve in cell cycle progression by regulating Cyclin E stability."

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"To prevent this degradation, USP27 interacts with and deubiquitinates cyclin E [66]."

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"First, USP27 interacts with and colocalizes with Cyclin E. Second, USP27 negatively regulates Cyclin E ubiquitination."
USP27X increases the amount of Cyclin_E.
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USP27X increases the amount of Cyclin_E. 1 / 1
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"Third, USP27 positively regulates Cyclin E protein level."
USP27X affects ATXN7L3
2 | 5 2
USP27X binds ATXN7L3.
2 | 4 2
2 | 3

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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations (XREF_FIG, lanes 5 and 6)."

No evidence text available

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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations."

No evidence text available

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"ATXN7L3 and ENY2 associate with USP27X and USP51."
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
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"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
USP27X deubiquitinates ATXN7L3.
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USP27X deubiquitinates ATXN7L3. 1 / 1
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"Interestingly, USP27x has been reported to deubiquitinate histone H2B-K120 in vivo and in vitro as part of a complex with ATXN7L3 and ENY2 (Atanassov et al., 2016), two of the three adapter proteins that are part of the USP22 DUB module."
ATXN7L3 affects USP27X
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ATXN7L3 binds USP27X.
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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations (XREF_FIG, lanes 5 and 6)."

No evidence text available

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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations."

No evidence text available

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"ATXN7L3 and ENY2 associate with USP27X and USP51."
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
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"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
ATXN7L3 deubiquitinates USP27X.
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ATXN7L3 deubiquitinates USP27X. 1 / 1
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"Our results now reveal that in addition to USP22, ATXN7L3 and ENY2 activate two previously uncharacterized deubiquitinating enzymes, USP27X and USP51, which are not part of SAGA."
USP51 affects USP27X
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USP51 binds USP27X. 4 / 4
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sparser
"The reduced tumor burden upon depletion of USP27X prompted us to search the The Cancer Genome Atlas (TCGA) database to see if altered expression of USP27X or USP51 is associated with certain cancer phenotypes."

sparser
"Interestingly, one of the USP27X and USP51 associated proteins, C1QBP, was originally described as a mitochondrial protein ( Dedio et al., 1998 )."

sparser
"Interestingly, one of the USP27X and USP51 associated proteins, C1QBP, was originally described as a mitochondrial protein ( xref )."

sparser
"The reduced tumor burden upon depletion of USP27X prompted us to search The Cancer Genome Atlas (TCGA) database to see if altered expression of USP27X or USP51 is associated with certain cancer phenot[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
USP22 binds USP51 and USP27X. 1 / 1
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sparser
"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
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"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances apoptosis."

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"Finally, deletion of Usp27x reduces apoptosis in NSCLC cells treated with an EGFR inhibitor."

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"However, the authors also found that overexpression of USP27x combined with ERK1/2 pathway inhibition to promote apoptosis."

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"Overexpression of Usp27x induces low levels of apoptosis in melanoma and non small cell lung cancer (NSCLC) cells and substantially enhances apoptosis induced in these cells by the inhibition of ERK signalling."

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"Overexpression of USP27x combined with ERK1/2 activation to promote the deubiquitylation and stabilisation of BIM and increase caspase‐dependent apoptosis."
Modified USP27X activates apoptotic process. 1 / 1
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"Overexpression of Usp27x reduces ERK dependent Bim ubiquitination, stabilizes phosphorylated Bim, and induces apoptosis in PMA stimulated cells, as well as in tumour cells with a constitutively active Raf and ERK pathway."
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"In addition, in NSCLC cells, depletion of USP27x reduces apoptosis when treated with an EGFR inhibitor."
USP27X affects USP51
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USP51 binds USP27X. 4 / 4
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sparser
"The reduced tumor burden upon depletion of USP27X prompted us to search the The Cancer Genome Atlas (TCGA) database to see if altered expression of USP27X or USP51 is associated with certain cancer phenotypes."

sparser
"Interestingly, one of the USP27X and USP51 associated proteins, C1QBP, was originally described as a mitochondrial protein ( Dedio et al., 1998 )."

sparser
"Interestingly, one of the USP27X and USP51 associated proteins, C1QBP, was originally described as a mitochondrial protein ( xref )."

sparser
"The reduced tumor burden upon depletion of USP27X prompted us to search The Cancer Genome Atlas (TCGA) database to see if altered expression of USP27X or USP51 is associated with certain cancer phenot[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
USP22 binds USP51 and USP27X. 1 / 1
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sparser
"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
USP27X affects ENY2
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USP27X binds ENY2.
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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations."

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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations (XREF_FIG, lanes 5 and 6)."

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"ATXN7L3 and ENY2 associate with USP27X and USP51."
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
| 1

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"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
USP27X deubiquitinates ENY2.
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USP27X deubiquitinates ENY2. 1 / 1
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"Interestingly, USP27x has been reported to deubiquitinate histone H2B-K120 in vivo and in vitro as part of a complex with ATXN7L3 and ENY2 (Atanassov et al., 2016), two of the three adapter proteins that are part of the USP22 DUB module."
USP22 affects USP27X
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USP22 binds USP27X.
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1 |

No evidence text available
USP22 binds USP51 and USP27X. 1 / 1
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sparser
"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
USP22 binds USP27X. 1 / 1
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"All these results indicate that USP27X and the close homologue USP22 specifically interact and stabilize Snail1."
USP22 inhibits USP27X.
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USP22 inhibits USP27X. 2 / 2
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"To determine whether USP22 blocks association of USP27X and USP51 with SAGA, we isolated GCN5 associated proteins after shRNA mediated depletion of USP22 (XREF_FIG, lanes 2 and 3 and 5 and 6)."

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"To determine whether USP22 blocks association of USP27X and USP51 with SAGA, we isolated GCN5 associated proteins after shRNA mediated depletion of USP22."
USP22 activates USP27X.
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USP22 activates USP27X. 2 / 2
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"Equal numbers of cells expressing shRNAs that specifically target USP27X or USP51, but not USP22, or expressing control shRNA, were seeded and monitored for proliferation by cell counts 72 hr later."

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"Equal numbers of cells expressing shRNAs that specifically target USP27X or USP51, but not USP22 (XREF_FIG), or expressing control shRNA, were seeded and monitored for proliferation by cell counts 72 hours later."
TGFB affects USP27X
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TGFB activates USP27X.
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TGFB activates USP27X. 6 / 6
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eidos
"USP27X can also deubiquitinate and stabilize Snail1 when induced by TGF-beta and therefore promotes EMT and tumor metastasis [ 53 ] ."

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"USP27X was upregulated by TGFbeta during EMT and was required for TGFbeta induced expression of Snail1 and other mesenchymal markers in epithelial cells and CAF."

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"In fact, DUBs involved in Snail regulation so far are shown to be induced differently, while USP27x is induced by TGF-β; DUB3/USP17L2 seems to play a role in CDK4/6-mediated activation of EMT, whereas OTUB1 is under the transcriptional regulation of oestrogen-related receptor alpha, and USP37 regulation is induced during EMT via the stimulation of the hedgehog signalling pathway."

eidos
"TGFbeta also induces USP27X expression , which increases SNAI1 stability by deubiquitination [ 55 ] ."
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"TGFbeta activated USP27X deubiquitinase regulates cell migration and chemoresistance via stabilization of Snail1."

eidos
"TGFbeta enhances USP27X expression that deubiquitinates and stabilizes Snail1 , which in turn induces EMT in cancer cells and activation of CAFs ."
TGFB increases the amount of USP27X.
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TGFB increases the amount of USP27X. 1 / 1
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"Specifically, DUB3 was shown to respond to IL-6-stimulated transcriptional activation and stabilize Snail1 in breast cancer cells; while USP27X expression was reported to be induced by TGFβ, which assisted the upregulation of Snail1 and other mesenchymal genes ."
HDAC1 affects USP27X
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HDAC1 inhibits USP27X. 7 / 7
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"As shown in Figure 5B, hD1 inhibits the USP27x complex at >25-fold higher inhibitor concentrations and modestly inhibits the USP51 complex only at >2500-fold higher concentration than that needed to inhibit the human DUB module."

sparser
"As shown in xref , hD1 inhibits the USP27x complex at >25-fold higher inhibitor concentrations and modestly inhibits the USP51 complex only at >2500-fold higher concentration than that needed to inhibit the human DUB module."

eidos
"In addition , the finding that hD1 inhibits USP27x alone as well as the USP27x / ENY2 / ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain , rather than to the ENY2 and ATXN7L3 subunits ."

sparser
"Since hD1 inhibits USP27x whether or not it is in complex with the other SAGA subunits, the inhibitor likely binds directly to the catalytic USP domain."

sparser
"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."

eidos
"Since hD1 inhibits USP27x whether or not it is in complex with the other SAGA subunits , the inhibitor likely binds directly to the catalytic USP domain ."

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"Since hD1 inhibits USP27x whether or not it is in complex with the other SAGA subunits, the inhibitor likely binds directly to the catalytic USP domain."
ENY2 affects USP27X
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ENY2 binds USP27X.
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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations."

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"As expected, ATXN7L3 and ENY2 associated with USP27X and USP51, but no other SAGA components, such as GCN5 or TAF10, were observed in the immunoprecipitations (XREF_FIG, lanes 5 and 6)."

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"ATXN7L3 and ENY2 associate with USP27X and USP51."
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
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sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
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"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
ENY2 deubiquitinates USP27X.
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ENY2 deubiquitinates USP27X. 1 / 1
| 1

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"Our results now reveal that in addition to USP22, ATXN7L3 and ENY2 activate two previously uncharacterized deubiquitinating enzymes, USP27X and USP51, which are not part of SAGA."
| 6
USP27X inhibits cell growth.
| 3
| 3

reach
"Ablation of USP27X leads to enhanced CCND1 ubiquitination, a drastic reduction in CCND1 protein levels, and abrogated cell growth in several cancer cell lines, including HER2 therapy resistant breast cancer cells and xenograft tumors."

reach
"These experiments confirmed that ablation of USP27X strongly impairs cell growth, whereas ATXN7L3 depletion has no impact (Supplementary Fig. 1)."

reach
"As shown in Figures 5I, J, L and M, expression of WT USP27X led to a significant increase in colony number, while expression of the catalytically inactive DUB suppressed cell growth in both lines."
USP27X activates cell growth.
| 3
| 3

reach
"USP27 knockdown inhibits HCC cell growth in vivo."

reach
"These results indicate that depletion of USP27 also inhibited HCC cell growth in vivo."

reach
"Herein, we demonstrate that USP27 regulates Cyclin E abundance to accelerate cell cycle progression, cell proliferation, and tumor cell growth as well."
USP27X affects TRIM28
| 1 5
USP27X binds TRIM28.
| 5
| 5

sparser
"At endogenous levels, the interaction between Usp27x L and TRIM28 was detected in 293FT cells (Fig.  xref D), but not in WM1158 cells (data not shown), which express substantially less Usp27x L compared to 293FT cells (Fig.  xref B)."

sparser
"Usp27x interacts with the E3-ubiquitin ligase TRIM28, and TRIM28 deficiency blocks Usp27x-induced loss of cFLIP L level and apoptosis induction by pIC."

sparser
"Instead, Usp27x interacted with the E3-ligase TRIM28 and reduced ubiquitination of TRIM28."

sparser
"We also could not detect an interaction between endogenous Usp27x and TRIM28 in WM1158 cells (data not shown), and Usp27x-deficient WM1158 cells were not protected from pIC-induced apoptotic cell death (Fig.  xref E)."

sparser
"However, in 293FT, which express substantially more Usp27x L (Fig.  xref B), the interaction between endogenous Usp27x and TRIM28 could be observed by IP (Fig.  xref D)."
USP27X deubiquitinates TRIM28.
| 1
USP27X leads to the deubiquitination of TRIM28. 1 / 1
| 1

reach
"Instead, Usp27x interacted with the E3-ligase TRIM28 and reduced ubiquitination of TRIM28."
| 1 5
| 1 4

reach
"Furthermore, evidence from in vitro and in vivo studies revealed that depletion of USP27 inhibited HCC cell proliferation, invasion, metastasis and tumorigenesis, and that overexpression of SETD3 rescued this phenotype."

eidos
"USP27X can also deubiquitinate and stabilize Snail1 when induced by TGF-beta and therefore promotes EMT and tumor metastasis [ 53 ] ."

reach
"Taken together, these results suggested that USP27 might promote hepatoma metastasis."

reach
"Although Cyclin E has been reported to involve in metastasis [XREF_BIBR], how USP27 promotes migration and metastasis also need further detailed exploration."

reach
"How does USP27 promote migration and metastasis?"
| 1

reach
"Down regulation of USP27 suppresses hepatocellular migration and metastasis."
BCL2L11 affects USP27X
3 | 2 1
3 | 2

No evidence text available

reach
"USP27x, acting as a tumor suppressor, could bind to Bim upon its anti-apoptotic ERK dependent phosphorylation and counteract the following proteasomal degradation via its deubiquitinase activity."

No evidence text available

No evidence text available

reach
"Furthermore, like βTrCP1/2, the binding of USP27x to BIM was dependent upon ERK1/2 activation."
| 1

sparser
"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."
USP27X affects cell cycle
| 5
| 5

reach
"We found that USP27 knockdown suppresses cell cycle progression by increasing the percentage of cells in G0/G1 phase, which can be reversed by the addition of Cyclin E expression."

reach
"Herein, we demonstrate that USP27 regulates Cyclin E abundance to accelerate cell cycle progression, cell proliferation, and tumor cell growth as well."

reach
"The observation that USP27 promotes cell cycle progression and cell proliferation prompted us to imagine that depletion of USP27 expression might suppress tumor progression."

reach
"To further support our notion that USP27 promotes cell cycle progression, we detected a statistically significant reduction in the growth of Hep3B and MHCC97H cells compared with that of control cells with single stable knockdown of USP27."

reach
"XREF_FIG, USP27 knockdown suppresses cell cycle progression by increasing the percentage of cells in G1/S phase but decreasing the percentage of cells in G2/M phase, similar to 5-FU treatment."

reach
"Upregulation of USP27 in hepatocellular carcinoma patients leads to elevated SETD3 expression and increased cell proliferation, invasion, migration and tumorigenesis."

reach
"USP27X modulates tumor chemoresistance and invasion through deubiquitination and stabilization of Snail1 XREF_BIBR."

reach
"Taken together, these data revealed that knockdown of USP27 or SETD3 prevents liver cancer cell migration and invasion."

reach
"Conversely, overexpression of USP27 evidently enhanced cell invasion."

reach
"Furthermore, evidence from in vitro and in vivo studies revealed that depletion of USP27 inhibited HCC cell proliferation, invasion, metastasis and tumorigenesis, and that overexpression of SETD3 rescued this phenotype."
TRIM28 affects USP27X
| 5
| 5

sparser
"At endogenous levels, the interaction between Usp27x L and TRIM28 was detected in 293FT cells (Fig.  xref D), but not in WM1158 cells (data not shown), which express substantially less Usp27x L compared to 293FT cells (Fig.  xref B)."

sparser
"Usp27x interacts with the E3-ubiquitin ligase TRIM28, and TRIM28 deficiency blocks Usp27x-induced loss of cFLIP L level and apoptosis induction by pIC."

sparser
"Instead, Usp27x interacted with the E3-ligase TRIM28 and reduced ubiquitination of TRIM28."

sparser
"We also could not detect an interaction between endogenous Usp27x and TRIM28 in WM1158 cells (data not shown), and Usp27x-deficient WM1158 cells were not protected from pIC-induced apoptotic cell death (Fig.  xref E)."

sparser
"However, in 293FT, which express substantially more Usp27x L (Fig.  xref B), the interaction between endogenous Usp27x and TRIM28 could be observed by IP (Fig.  xref D)."
Cyclin_E affects USP27X
| 5
Cyclin_E binds USP27X.
| 4

reach
"To prevent this degradation, USP27 interacts with and deubiquitinates cyclin E [66]."

reach
"The observation that USP27 interacts with and deubiquitinates Cyclin E led us to think that USP27 might involve in cell cycle progression by regulating Cyclin E stability."

reach
"In addition, we examined whether endogenous Cyclin E interacts with USP27 in the Hep3B cells."

reach
"To further confirm that the interaction between Cyclin E and USP27 was specific, we transfected them alone or together into HEK293T cells and evaluated their interaction by immunoprecipitation and WB."
Cyclin_E inhibits USP27X.
| 1
| 1

reach
"Interestingly, USP27 expression might also be regulated by Fbxw7, a well-known E3 ubiquitin ligase of Cyclin E, which interacts with and degrades USP27."
| 4
USP27X activates cell migration.
| 3

reach
"Furthermore, USP27 or SETD3 knockdown inhibits cell proliferation, cell migration and tumorigenesis, while overexpression of SETD3 in USP27-deficient HCC cells could restore cell viability."

reach
"Taken together, these data revealed that knockdown of USP27 or SETD3 prevents liver cancer cell migration and invasion."

reach
"To explore the roles of the USP27–SETD3 axis in cell migration and invasion, we performed the wound-healing assay and the results showed that knockdown of SETD3 or USP27 significantly inhibited cell migration compared to that in the control cells, whereas introducing SETD3 into USP27 knockdown cells partially restored the metastatic phenotype (Fig. 6A-D)."
| 1

reach
"As shown in Figure S5A-D, depletion of USP27 expression significantly decreased cell migration compared with the control in Hep3B and MHCC97H cells using wound healing assay."
USP27X affects FAM126A
| 4
| 4

reach
"We also found that the levels of SETD3 and USP27 increased significantly in HCC than those in the relevant adjacent tissues."

reach
"Furthermore, evidence from in vitro and in vivo studies revealed that depletion of USP27 inhibited HCC cell proliferation, invasion, metastasis and tumorigenesis, and that overexpression of SETD3 rescued this phenotype."

reach
"USP27 knockdown inhibits HCC cell growth in vivo."

reach
"These results indicate that depletion of USP27 also inhibited HCC cell growth in vivo."
3 |
Valproic acid decreases the amount of USP27X.
2 |
Valproic acid decreases the amount of USP27X. 2 / 2
2 |

No evidence text available

No evidence text available
Valproic acid methylates USP27X.
1 |
1 |

No evidence text available
USP27X affects USP22
1 | 2
1 |

No evidence text available
USP22 binds USP51 and USP27X. 1 / 1
| 1

sparser
"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
USP22 binds USP27X. 1 / 1
| 1

sparser
"All these results indicate that USP27X and the close homologue USP22 specifically interact and stabilize Snail1."
| 3
USP27X deubiquitinates Histone_H2B. 3 / 3
| 3

reach
"Remarkably, this inhibitor also showed greater activity on USP22 than on two other DUBs, USP27x and USP51, that also deubiquitinate histone H2B and form complexes with two of the SAGA DUB module adaptor subunits."

reach
"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that the ATXN7L3 zinc finger plays a role analogous to that of the Sgf11 zinc finger in docking human SAGA DUB [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that all three use the ATXN7L3 zinc finger to dock the H2A and H2B acidic patch in a manner similar to that shown in the structure of the yeast DUB module bound to ubiquitinated nucleosomes."
USP27X affects DDX58
| 3
USP27X ubiquitinates DDX58.
| 2
USP27X ubiquitinates DDX58. 2 / 2
| 2

reach
"To the best of our knowledge, at least nine DUBs, A20, CYLD, USP3, USP5, USP14, USP15, USP21, USP25, and USP27X, have been proposed to counteract the K63linked ubiquitination of RIG-I and, thereby attenuate downstream signaling and IFN-b production ( Table 1 and Figure 3 ) (58, 76, 93) ."

reach
"USP27X negatively regulates antiviral signaling by deubiquitinating RIG-I."
USP27X deubiquitinates DDX58.
| 1
USP27X leads to the deubiquitination of DDX58. 1 / 1
| 1

reach
"Additionally, ubiquitination assays demonstrated that USP27X reduced RIG-I ubiquitination, specifically the K63-ubiquitin linkage type."
| 3

reach
"Furthermore, evidence from in vitro and in vivo studies revealed that depletion of USP27 inhibited HCC cell proliferation, invasion, metastasis and tumorigenesis, and that overexpression of SETD3 rescued this phenotype."

reach
"Furthermore, USP27 or SETD3 knockdown inhibits cell proliferation, cell migration and tumorigenesis, while overexpression of SETD3 in USP27-deficient HCC cells could restore cell viability."

reach
"Upregulation of USP27 in hepatocellular carcinoma patients leads to elevated SETD3 expression and increased cell proliferation, invasion, migration and tumorigenesis."
USP27X affects CGAS
| 3
USP27X binds CGAS.
| 2
USP27X binds CGAS and K48. 2 / 2
| 2

reach
"In this study, we identified that deubiquitinase USP27X could interact with cGAS and cleave K48 linked polyubiquitination chains from cGAS, leading to cGAS stabilization."

reach
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48 linked polyubiquitin chains during viral infection."
USP27X deubiquitinates CGAS.
| 1
USP27X deubiquitinates CGAS. 1 / 1
| 1

reach
"Cutting Edge : USP27X Deubiquitinates and Stabilizes the DNA Sensor cGAS to Regulate Cytosolic DNA Mediated Signaling."
PLEC affects USP27X
| 3
PLEC inhibits USP27X. 3 / 3
| 3

sparser
"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."

sparser
"As shown in xref , hD1 inhibits the USP27x complex at >25-fold higher inhibitor concentrations and modestly inhibits the USP51 complex only at >2500-fold higher concentration than that needed to inhibit the human DUB module."

sparser
"Since hD1 inhibits USP27x whether or not it is in complex with the other SAGA subunits, the inhibitor likely binds directly to the catalytic USP domain."
ENY2 affects ATXN7L3
| 1 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
| 1

reach
"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
2 |
Hsa-miR-8485 decreases the amount of USP27X. 2 / 2
2 |

No evidence text available

No evidence text available
2 |
Hsa-miR-552-5p decreases the amount of USP27X. 2 / 2
2 |

No evidence text available

No evidence text available
2 |
Hsa-miR-302c-5p decreases the amount of USP27X. 2 / 2
2 |

No evidence text available

No evidence text available
CGAS affects USP27X
| 2
USP27X binds cGAS. 2 / 2
| 2

sparser
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48‐linked polyubiquitin chains during viral infection.[ 208 ] Recently, a study reported that USP29 interacts with cGAS, hydrolyzes K48‐linked polyubiquitin chains on cGAS, and stabilizes cGAS in uninfected cells, or after HSV‐1 stimulation.[ 209 ] Following HSV‐1 infection, USP29 knockout mice were shown to be hypersensitive to HSV‐1 and produced less type I IFNs and proinflammatory cytokines than the wildtype control."

sparser
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48‐linked polyubiquitin chains during viral infection. [ xref ] Recently, a study reported that USP29 interacts with cGAS, hydrolyzes K48‐linked polyubiquitin chains on cGAS, and stabilizes cGAS in uninfected cells, or after HSV‐1 stimulation. [ xref ] Following HSV‐1 infection, USP29 knockout mice were shown to be hypersensitive to HSV‐1 and produced less type I IFNs and proinflammatory cytokines than the wildtype control."
2 |
Bisphenol A increases the amount of USP27X.
1 |
Bisphenol A increases the amount of USP27X. 1 / 1
1 |

No evidence text available
Bisphenol A decreases the amount of USP27X.
1 |
Bisphenol A decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
2 |
Benzo[a]pyrene decreases the amount of USP27X. 2 / 2
2 |

No evidence text available

No evidence text available
USP51 affects USP
| 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
USP27X affects cGAS
| 2
USP27X binds cGAS. 2 / 2
| 2

sparser
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48‐linked polyubiquitin chains during viral infection.[ 208 ] Recently, a study reported that USP29 interacts with cGAS, hydrolyzes K48‐linked polyubiquitin chains on cGAS, and stabilizes cGAS in uninfected cells, or after HSV‐1 stimulation.[ 209 ] Following HSV‐1 infection, USP29 knockout mice were shown to be hypersensitive to HSV‐1 and produced less type I IFNs and proinflammatory cytokines than the wildtype control."

sparser
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48‐linked polyubiquitin chains during viral infection. [ xref ] Recently, a study reported that USP29 interacts with cGAS, hydrolyzes K48‐linked polyubiquitin chains on cGAS, and stabilizes cGAS in uninfected cells, or after HSV‐1 stimulation. [ xref ] Following HSV‐1 infection, USP29 knockout mice were shown to be hypersensitive to HSV‐1 and produced less type I IFNs and proinflammatory cytokines than the wildtype control."
USP27X affects USP
| 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
USP27X affects Neoplasms
| 2
| 2

reach
"Importantly, dox-induced depletion of USP27X significantly impaired further tumor development."

reach
"Collectively, we revealed that USP27 exerts tumor-promoting action by modulating the USP27–SETD3 axis.Studies have validated that USP22, the USP27 homologous protein, has similar effects with USP27 [16, 21, 22]."
USP27X affects K48
| 2
USP27X binds CGAS and K48. 2 / 2
| 2

reach
"In this study, we identified that deubiquitinase USP27X could interact with cGAS and cleave K48 linked polyubiquitination chains from cGAS, leading to cGAS stabilization."

reach
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48 linked polyubiquitin chains during viral infection."
USP27X affects Histone
| 2
USP27X deubiquitinates Histone. 2 / 2
| 2

reach
"Interestingly, our previous studies demonstrated that USP27X is inactive in insolation and cannot deubiquitinate histones or digest artificial substrates (such as Ub-AMC) in vitro unless bound by ATXN7L3 (23)."

reach
"Our previous work uncovered USP27X as an epigenetic modifier that deubiquitinates histone 2B (H2Bub1) and regulates gene transcription (23)."
USP27X affects HES1
1 | 1
USP27X deubiquitinates HES1. 2 / 2
1 | 1

"Knockdown of Usp22 shortened the half-life of Hes1, delayed its oscillation, and enhanced neuronal differentiation in mouse developing brain, whereas mis-expression of Usp27x reduced neuronal differentiation."

reach
"In addition, USP27 could regulate neuronal differentiation of stem cells in the developing mouse neocortex by deubiquitinating and stabilizing Hes1 [22]."
USP27X affects H2Bub1
| 2
USP27X deubiquitinates H2Bub1.
| 1
USP27X deubiquitinates H2Bub1. 1 / 1
| 1

reach
"Our previous work uncovered USP27X as an epigenetic modifier that deubiquitinates histone 2B (H2Bub1) and regulates gene transcription (23)."
USP27X activates H2Bub1.
| 1
USP27X activates H2Bub1. 1 / 1
| 1

reach
"Taken together with previous findings by others that USP22 is overexpressed in many cancers and our findings that ATXN7L3 and ENY2 levels are normally limiting in cells, these results suggest that imb[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP27X affects H2Aub1
| 2
USP27X deubiquitinates H2Aub1. 2 / 2
| 2

reach
"As was previously shown for the USP22 DUBm (Zhang et al., 2008a; Zhao et al., 2008), both USP27X and USP51 DUBm also deubiquitinated nucleosomal or free H2Aub1."

reach
"As was previously shown for the USP22 DUBm, both USP27X and USP51 DUBm also deubiquitinated nucleosomal or free H2Aub1 (XREF_FIG and XREF_SUPPLEMENTARY)."
USP affects USP51
| 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
SETD3 affects USP27X
| 2
SETD3 inhibits USP27X.
| 1
SETD3 inhibits USP27X. 1 / 1
| 1

reach
"Similarly, the decreased proliferation was also confirmed by Ki67 immunofluorescence staining as the proportions of Ki67-positive proliferating cells were significantly lower in USP27 or SETD3 knockdown cells, while SETD3 overexpression could increase Ki67-positive proliferating cells in USP27-deficient cells (Supplementary Fig. S2)."
SETD3 binds USP27X.
| 1
| 1

reach
"To further confirm that the interaction between SETD3 and USP27 was specific, we transfected them alone or together into 293 T cells and evaluated their interaction by immunoprecipitation and western blot."
K48 affects USP27X
| 2
USP27X binds CGAS and K48. 2 / 2
| 2

reach
"In this study, we identified that deubiquitinase USP27X could interact with cGAS and cleave K48 linked polyubiquitination chains from cGAS, leading to cGAS stabilization."

reach
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48 linked polyubiquitin chains during viral infection."
ENY2 affects USP51
| 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
EGFR inhibitor affects USP27X
| 2
EGFR inhibitor inhibits USP27X.
| 1
EGFR inhibitor inhibits USP27X. 1 / 1
| 1

reach
"Finally, deletion of Usp27x reduces apoptosis in NSCLC cells treated with an EGFR inhibitor."
EGFR inhibitor activates USP27X.
| 1
EGFR inhibitor activates USP27X. 1 / 1
| 1

reach
"In addition, in NSCLC cells, depletion of USP27x reduces apoptosis when treated with an EGFR inhibitor."
CGAS affects USP27X
| 2
USP27X binds CGAS and K48. 2 / 2
| 2

reach
"In this study, we identified that deubiquitinase USP27X could interact with cGAS and cleave K48 linked polyubiquitination chains from cGAS, leading to cGAS stabilization."

reach
"Unlike USP14, USP27x directly interacts with cGAS and releases the K48 linked polyubiquitin chains during viral infection."
CCND1 affects USP27X
| 2
CCND1 binds USP27X.
| 1
| 1

reach
"USP27X binds to and stabilizes CCND1 in a catalytically-dependent manner by negatively regulating its ubiquitination."
CCND1 activates USP27X.
| 1
CCND1 activates USP27X. 1 / 1
| 1

reach
"Additionally, expression of ectopic CCND1 almost completely rescued the growth defects in USP27X-depleted cells (Supplementary Fig. 5)."
ATXN7L3 affects USP51
| 2
USP27X binds USP51, ENY2, ATXN7L3, and USP. 2 / 2
| 2

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ 47 • ]."

sparser
"A recent study showed that ATXN7L3 and ENY2 can also form complexes with two additional USP DUBs, USP27x and USP51, and target them to H2B-Ub [ xref ]."
| 2
| 1

reach
"In our study, we found that both USP27 and Cyclin E are downregulated by 5-FU treatment in a dose dependent manner."
5-formyluracil decreases the amount of USP27X.
| 1
5-formyluracil decreases the amount of USP27X. 1 / 1
| 1

reach
"Anti-cancer drug 5-FU regulates cell cycle progression and inhibits hepatocellular proliferation by downregulating USP27 expression."
Urethane affects USP27X
1 |
Urethane decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
Superoxide affects USP27X
| 1
| 1

reach
"Down-regulation of Raptor expression increased mitochondrial ROS production, and mitochondria specific superoxide scavengers prevented USP27x mediated stabilization of Bim by inhibition of Cat K. Moreover, combined treatment with Cat K inhibitor (odanacatib) and tumor necrosis factor related apoptosis inducing ligand (TRAIL) reduced tumor growth and induced cell death in a xenograft model."
Sunitinib affects USP27X
1 |
Sunitinib decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
Silver(0) affects USP27X
1 |
Silver(0) decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
Proteasome inhibitor affects USP27X
| 1
Proteasome inhibitor activates USP27X. 1 / 1
| 1

reach
"XREF_FIG, MG132 (proteasome inhibitor) treatment could rescue the USP27 knockdown mediated degradation of Cyclin E protein."
Potassium dichromate increases the amount of USP27X. 1 / 1
1 |

No evidence text available
Jinfukang affects USP27X
1 |
Jinfukang increases the amount of USP27X. 1 / 1
1 |

No evidence text available
1 |
Hsa-miR-603 decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
Dieldrin affects USP27X
1 |
Dieldrin increases the amount of USP27X. 1 / 1
1 |

No evidence text available
Dibutyl phthalate decreases the amount of USP27X. 1 / 1
1 |

No evidence text available
Cisplatin affects USP27X
1 |
Cisplatin increases the amount of USP27X. 1 / 1
1 |

No evidence text available
USP51 affects USP22
| 1
USP22 binds USP51 and USP27X. 1 / 1
| 1

sparser
"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
USP27X affects ~3
| 1
USP27X inhibits ~3. 1 / 1
| 1

reach
"USP27X-depleted tumors weighed ~3 fold less than control tumors (Supplementary Fig. 4)."
USP27X affects tumor cell growth
| 1
USP27X activates tumor cell growth. 1 / 1
| 1

eidos
"Here , we reported that ubiquitin-specific peptidase 27 ( USP27 ) promotes tumor cell growth by specifically interacting with SETD3 , negatively regulating its ubiquitination , and enhancing its stability ."
USP27X affects stabilization Bim
| 1
USP27X activates stabilization Bim. 1 / 1
| 1

eidos
"Weber et al. reported that USP27x induced stabilization of Bim [ 27 ] ."
USP27X affects opening molecules
| 1
USP27X inhibits opening molecules. 1 / 1
| 1

eidos
"Inhibition of USP27X enhanced cell death promoted by exposition to cisplatin [ 5 ] , opening the possibility to use small molecules against this enzyme to restore or potentiate chemosensitivy to cisplatin or other drugs ."
| 1

reach
"Knockout mice have not been generated; however, overexpression of Usp27x inhibits neurogenesis in mice (44)."

eidos
"USP27X can also deubiquitinate and stabilize Snail1 when induced by TGF-beta and therefore promotes EMT and tumor metastasis [ 53 ] ."
USP27X affects cisplatin
| 1
| 1

reach
"USP27X depletion impaired Snail1 dependent cell migration and invasion and metastasis formation and increased cellular sensitivity to cisplatin."
USP27X affects cell tumorigenesis carcinoma
| 1
USP27X activates cell tumorigenesis carcinoma. 1 / 1
| 1

eidos
"Inhibition of USP27 expression led to the downregulation of SETD3 protein level , the blockade of the cell proliferation and tumorigenesis of hepatocellular carcinoma ( HCC ) cells ."

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"Knockdown of Usp22 shortened the half-life of Hes1, delayed its oscillation, and enhanced neuronal differentiation in mouse developing brain, whereas mis expression of Usp27x reduced neuronal differentiation."
USP27X affects cell death
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"Inhibition of USP27X enhanced cell death promoted by exposition to cisplatin [5], opening the possibility to use small molecules against this enzyme to restore or potentiate chemosensitivy to cisplatin or other drugs.Recently, Dub3 was also described as a deubiquitinase of Snail1 [9]."
USP27X affects cell death exposition
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USP27X inhibits cell death exposition. 1 / 1
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eidos
"Inhibition of USP27X enhanced cell death promoted by exposition to cisplatin [ 5 ] , opening the possibility to use small molecules against this enzyme to restore or potentiate chemosensitivy to cisplatin or other drugs ."
USP27X affects cdk-4
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USP27X increases the amount of cdk-4. 1 / 1
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"Figure 2F confirms that USP27X loss causes a substantial reduction of CCND1, but not CCND3, CCNE1, or CDK4/6 protein levels in these cells."
USP27X affects Ubiquitin
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"In the past year, two other deubiquitinating enzymes, USP27X and USP1, have been reported to impede ubiquitin mediated degradation of Snail1 in various biological contexts XREF_BIBR, XREF_BIBR."
USP27X affects UBC
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No evidence text available
USP27X affects TBCEL
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sparser
"Furthermore, like βTrCP1/2, the binding of USP27x to BIM EL was dependent upon ERK1/2 activation."
USP27X affects Snail1
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USP27X deubiquitinates Snail1. 1 / 1
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"USP27X can also deubiquitinate and stabilize Snail1 when induced by TGF-beta and therefore promotes EMT and tumor metastasis [XREF_BIBR]."
USP27X affects Snail1 protein
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USP27X inhibits Snail1 protein. 1 / 1
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"Accordingly, downregulation of USP27X decreased Snail1 protein in several tumor cell lines."
USP27X affects SNAI1
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USP27X deubiquitinates SNAI1. 1 / 1
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"3) Does USP27X require specific cofactors to deubiquitinate Snail1?"
USP27X affects SNAI1 stability
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USP27X activates SNAI1 stability. 1 / 1
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eidos
"TGFbeta also induces USP27X expression , which increases SNAI1 stability by deubiquitination [ 55 ] ."
| PMC
USP27X affects SH3KBP1
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No evidence text available
USP27X affects SETD3 protein
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USP27X activates SETD3 protein. 1 / 1
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eidos
"Inhibition of USP27 expression led to the downregulation of SETD3 protein level , the blockade of the cell proliferation and tumorigenesis of hepatocellular carcinoma ( HCC ) cells ."
USP27X affects RTL10
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USP27X deubiquitinates RTL10. 1 / 1
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"Moreover, USP27 deubiquitinates and stabilizes the BH3-only protein Bim, subsequently enhancing apoptosis [14]."
USP27X affects RNF168
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USP27X activates RNF168. 1 / 1
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"Interestingly, the DUBs USP26 and USP27 were found to modulate RNF168 mediated protein ubiquitylation at DSB sites, preventing excessive spreading of RAP80-BRCA1, promoting association of BRCA1 with P[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP27X affects RIG-I ubiquitination
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USP27X inhibits RIG-I ubiquitination. 1 / 1
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eidos
"Additionally , ubiquitination assays demonstrated that USP27X reduced RIG-I ubiquitination , specifically the K63-ubiquitin linkage type ."
USP27X affects RB1
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USP27X leads to the phosphorylation of RB1. 1 / 1
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"As expected, USP27X depletion substantially reduced both CCND1 levels and Rb1 phosphorylation in these cells (Fig. 5E, compare lane 1 to 2)."
USP27X affects RAF
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USP27X inhibits RAF. 1 / 1
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"Loss of endogenous Usp27x enhances the Bim degrading activity of oncogenic Raf."
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"Overexpression of the Ubiquitin Specific Proteases USP43, USP41, USP27x and USP6 in Osteosarcoma Cell Lines: Inhibition of Osteosarcoma Tumor Growth and Lung Metastasis Development by the USP Antagonist PR619."
USP27X affects Mice
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USP27X inhibits Mice. 1 / 1
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"Knockout mice have not been generated; however, overexpression of Usp27x inhibits neurogenesis in mice (44)."
USP27X affects KLHL20
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No evidence text available
USP27X affects Interferon
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"Among the DUBs that interact with cGAS or MDA5, USP27X (98) and USP29 (99) stabilize cGAS and thus positively regulate IFN production and antiviral activities."
USP27X affects ITCH
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sparser
"Although we did not detect binding between Usp27x L and CHIP by co-IP, there was a clear interaction of Usp27x L with Itch and also (although less pronounced) with DTX1 (Supplementary Fig. S6B)."
USP27X affects H2BC10
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USP27X deubiquitinates H2BC10. 1 / 1
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"In contrast, depletion of non-enzymatic components, ATXN7L3 or ENY2, results in increased H2Bub1. These observations led us to discover two H2Bub1 DUBs, USP27X and USP51, which function independently of SAGA and compete with USP22 for ATXN7L3 and ENY2 for activity."
USP27X affects GATD3B
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USP27X deubiquitinates GATD3B. 1 / 1
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"We found that Hes1 was deubiquitinated and stabilized by Usp27x and its homologs ubiquitin specific protease 22 (Usp22) and ubiquitin specific protease 51 (Usp51)."
USP27X affects ERK
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sparser
"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."
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"As shown in Fig. 4A and B, USP27 knockdown markedly reduce the cell viability of Hep3B and MHCC97H cells."
USP27X affects Caspase
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"Overexpression of USP27x combined with ERK1/2 activation to promote the deubiquitylation and stabilisation of BIM and increase caspase‐dependent apoptosis."
USP27X affects CFLAR
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USP27X decreases the amount of CFLAR. 1 / 1
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"Here, we report that enhanced expression of Usp27x in human melanoma cells leads to the loss of cellular FLICE-like inhibitory protein (cFLIP) and sensitizes to Tumor necrosis factor receptor 1 (TNF-R1) or Toll-like receptor 3 (TLR3)-induced extrinsic apoptosis through enabling enhanced processing of caspase-8."
USP27X affects BTRC
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sparser
"IκBα-degradation is achieved through the activity of the E3-ubiquitin ligase complex SCF β-TRCP [ xref ], and it has been reported that Usp27x can bind β-TrCP [ xref , xref ]."
USP22 affects USP51
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USP22 binds USP51 and USP27X. 1 / 1
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"Due to the lack of ChIP grade antibodies, we have not yet been able to define loci directly bound by USP27X, USP51, or USP22, so we cannot specify genes and pathways directly governed by these DUBs."
UBC affects USP27X
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No evidence text available
TBCEL affects USP27X
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sparser
"Furthermore, like βTrCP1/2, the binding of USP27x to BIM EL was dependent upon ERK1/2 activation."
Soman affects USP27X
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Soman increases the amount of USP27X. 1 / 1
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No evidence text available
SH3KBP1 affects USP27X
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No evidence text available
N-methyl-4-phenylpyridinium increases the amount of USP27X. 1 / 1
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No evidence text available
KLHL20 affects USP27X
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No evidence text available
ITCH affects USP27X
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sparser
"Although we did not detect binding between Usp27x L and CHIP by co-IP, there was a clear interaction of Usp27x L with Itch and also (although less pronounced) with DTX1 (Supplementary Fig. S6B)."
ERK affects USP27X
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sparser
"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."
CAT affects USP27X
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CAT decreases the amount of USP27X. 1 / 1
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"Inhibition of Cat K increased USP27x expression, and knock down of USP27x markedly blocked Cat K induced up-regulation of Bim expression."
BTRC affects USP27X
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sparser
"IκBα-degradation is achieved through the activity of the E3-ubiquitin ligase complex SCF β-TRCP [ xref ], and it has been reported that Usp27x can bind β-TrCP [ xref , xref ]."
BCL2L11 affects ERK, and USP27X
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sparser
"Here, we report the identification of a deubiquitinase, Usp27x, that binds Bim upon its ERK-dependent phosphorylation and can upregulate its expression levels."
ATXN7L3 affects ENY2, and USP27X
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"In addition, the finding that hD1 inhibits USP27x alone as well as the USP27x/ENY2/ATXN7L3 complex suggest that hD1 inhibits DUB activity by binding directly to the catalytic domain, rather than to the ENY2 and ATXN7L3 subunits."
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No evidence text available