IndraLab

Statements

USP27X affects 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."
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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."
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USP27X affects 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."
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"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."
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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."
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USP27X affects 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)."
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USP27X affects Histone_H2B
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USP27X deubiquitinates Histone_H2B. 3 / 3
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"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."
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"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]"
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"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."
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USP27X affects 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."
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USP27X affects Histone
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USP27X deubiquitinates Histone. 2 / 2
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"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)."
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"Our previous work uncovered USP27X as an epigenetic modifier that deubiquitinates histone 2B (H2Bub1) and regulates gene transcription (23)."
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USP27X affects HES1
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USP27X deubiquitinates HES1. 2 / 2
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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."
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"In addition, USP27 could regulate neuronal differentiation of stem cells in the developing mouse neocortex by deubiquitinating and stabilizing Hes1 [22]."
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USP27X affects H2Aub1
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USP27X deubiquitinates H2Aub1. 2 / 2
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"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."
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"As was previously shown for the USP22 DUBm, both USP27X and USP51 DUBm also deubiquitinated nucleosomal or free H2Aub1 (XREF_FIG and XREF_SUPPLEMENTARY)."
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USP27X affects TRIM28
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USP27X leads to the deubiquitination of TRIM28. 1 / 1
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"Instead, Usp27x interacted with the E3-ligase TRIM28 and reduced ubiquitination of TRIM28."
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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]."
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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?"
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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]."
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USP27X affects H2Bub1
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USP27X deubiquitinates H2Bub1. 1 / 1
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"Our previous work uncovered USP27X as an epigenetic modifier that deubiquitinates histone 2B (H2Bub1) and regulates gene transcription (23)."
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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."
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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)."
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USP27X affects 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."
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USP27X affects DDX58
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USP27X leads to the deubiquitination of DDX58. 1 / 1
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"Additionally, ubiquitination assays demonstrated that USP27X reduced RIG-I ubiquitination, specifically the K63-ubiquitin linkage type."
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USP27X affects CGAS
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USP27X deubiquitinates CGAS. 1 / 1
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"Cutting Edge : USP27X Deubiquitinates and Stabilizes the DNA Sensor cGAS to Regulate Cytosolic DNA Mediated Signaling."
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USP27X affects 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."
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