IndraLab
Statements
reach
"Considering that loss of PTEN contributed to fibroblasts phenotypic changes and USP13 interacted with PTEN and functioned as a deubiquitylase in epithelial cells, we subsequently sought to determine whether USP13 deficiency is responsible for the low PTEN expression observed in IPF fibroblasts."
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
reach
"Collectively, these data suggest that loss of USP13 may contribute to loss of PTEN in a substantial fraction of human tumors, whereas in other tumors PTEN can be inactivated by different mechanisms, including genetic alterations and upregulation of PTEN ubiquitin ligases (such as NEDD4-1 14 and WWP2 15)."
reach
"On the other hand, ectopic expression of wild-type USP13, but not the C345A mutant which is still capable of interacting with PTEN (XREF_FIG), reduced the poly-ubiquitination of PTEN by 65% (XREF_FIG), suggesting that the enzymatic activity of USP13 is indispensable for USP13 dependent deubiquitination of PTEN."
reach
"Two independent USP13 shRNAs both decreased PTEN protein expression by 80% and increased phospho-AKT and phospho-FOXO1/3 levels by 3- to 5-fold in SUM159 breast cancer cells, while restoration of PTEN or expression of an RNAi resistant ' silence mutant ' (i.e., no amino acid change) of USP13 (USP13-RE) in USP13 depleted SUM159 cells completely reversed the effect of USP13 shRNA on upregulating the phosphorylation of AKT and FOXO (XREF_FIG and XREF_SUPPLEMENTARY)."
sparser
"However, correlation analysis of RNA sequencing data from TCGA failed to provide evidence that USP13 and MCL1 were associated with each other at the messenger RNA (mRNA) level (Supplementary Fig. xref ), implying that USP13-mediated regulation of MCL1, if any, might not occur through a transcriptional mechanism."
reach
"Interestingly, Zhang et al. showed that pharmacological inhibition of USP13 by a small-molecule inhibitor, spautin-1, markedly downregulated MCL1 protein levels and sensitized ovarian and lung cancer cells to ABT-263, a selective antagonist of BCL-2 and BCL-XL.We selected DUB3 as an ideal target in ovarian cancer due to its oncogenic functions in various cancer subtypes ."
reach
"We confirmed the siRNA screen results by transfecting each of the four oligos against USP13 into HEK293T cells, and indeed found that USP13 knockdown decreased the endogenous protein levels of MCL1, while modulating USP9X or OTUB2 with different siRNAs had no consistent effects on MCL1 expression."
reach
"In addition, genetic depletion of USP13 using clustered regularly interspaced palindromic repeats (CRISPR)/Cas9, or pharmacological inhibition of USP13 by a small-molecule inhibitor spautin-1, markedly downregulates MCL1 protein expression and shows synergistic effects against tumor cells in combination with ABT-263, a selective antagonist of BCL-2 and BCL-XL."
reach
"Hence, pharmaceutical intervention of USP13 activity is expected to antagonize the tumorigenic potential of MCL1 oncoprotein, and combined administration of USP13 inhibitors with clinically approved venetoclax therapy may represent a promising targeting strategy for the treatment of human cancer by inducing tumor cell death."
sparser
"To investigate whether USP13 mediated the deubiquitination of cohesin subunits, we cotransfected 293T cells with expression vectors for His-ubiquitin and Myc-USP13, purified ubiquitinated proteins by Ni-NTA affinity chromatography, and performed Western blot with antibodies to SMC3 and RAD21 ( xref A )."
reach
"Collectively, these data demonstrate that the ubiquitination insensitive mutant of c-Myc is able to rescue the phenotypes caused by USP13 knockdown or FBXL14 overexpression in vitro and in vivo, which supports that USP13 and FBXL14 mediate posttranslational regulation of c-Myc to control the stem cell like phenotype and tumorigenic potential of GSCs."
reach
"As USP13 functions as a deubiquitinase that also interacts with c-Myc (XREF_FIG) and the preferential expression of USP13 in GSCs positively regulates c-Myc protein levels (XREF_FIG), we hypothesized that USP13 might mediate deubiquitination of c-Myc protein to prevent its degradation and stabilize c-Myc in GSCs."
"In this study, we demonstrate that the deubiquitinase USP13 stabilizes c-Myc by antagonizing FBXL14-mediated ubiquitination to maintain GSC self-renewal and tumorigenic potential."
reach
"As USP13 functions as a deubiquitinase that also interacts with c-Myc (XREF_FIG) and the preferential expression of USP13 in GSCs positively regulates c-Myc protein levels (XREF_FIG), we hypothesized that USP13 might mediate deubiquitination of c-Myc protein to prevent its degradation and stabilize c-Myc in GSCs."
reach
"Moreover, treatment with a proteasome inhibitor blocked the c-Myc loss caused by USP13 knockdown (not depicted), but overexpression of USP13 delayed c-Myc turnover in the presence of cycloheximide (not depicted), suggesting a critical role of USP13 in preventing proteasomal degradation of c-Myc in GSCs."
"While A20 inhibits PtdIns3P signaling by removing the TRAF6-dependent Lys63-linked chains from Beclin 1, the enzymes USP10 and USP13 prevent PI3K-III complex components from their degradation and, therefore, support autophagy. Interestingly enough, USP10 also stabilizes p53, which, in turn, triggers the degradation of Beclin 1 and VPS34 in order to prevent autophagy."
reach
"Conversely, it was show that Beclin 1 is deubiquitinated by USP10 and USP13 and adding complexity, Beclin 1 itself controlled the protein stabilities of USP10 and USP13 by regulating their deubiquitinating activities, in turn regulating the levels of tumor suppressor p53 [XREF_BIBR]."
USP13 is modified
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34
USP13 is phosphorylated.
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sparser
"As expected, USP13-Y708E transfection in HEK293 cells significantly inhibited the binding of c-Myc to Fbxl14, while USP13-Y708F significantly increased it (data not shown), revealing that USP13 phosphorylation at Y708 reverts c-Myc ubiquitination mediated by Fbxl14, thereby enhancing its stability ( xref )."
sparser
"We demonstrated that (1) a recurrent Q607R somatic substitution in CLK3 was identified in 8% of 100 human CCAs, particularly in patients with CCA metastasis; (2) the expression of CLK3 was significantly up-regulated in CCA compared with matched control tissues; (3) CLK3 knockdown significantly inhibited CCA aggressiveness in vitro and in vivo; (4) gene ontology term enrichment and MS assays indicated that high CLK3 expression in CCA patients mainly regulated nucleotide metabolism, especially purine biosynthesis; (5) mechanistically, CLK3 directly phosphorylated USP13 at Y708, which promoted its binding to c-Myc, a critical purine synthesis–associated transcription factor, thereby preventing Fbxl14-mediated c-Myc ubiquitination and activating the transcription of purine metabolic genes; (6) the CCA-associated CLK3-Q607R mutant induced USP13-Y708 phosphorylation and enhanced the activity of c-Myc; (7) in turn, c-Myc transcriptionally up-regulated CLK3; (8) importantly, levels of CLK3 significantly correlated with the expression of phospho-USP13-Y708, c-Myc, and ATIC in human CCA specimens; and (9) tacrine hydrochloride was identified as a potential compound to inhibit the aberrant CLK3-enhanced CCA invasiveness."
sparser
"Moreover, ATM-induced phosphorylation of the Thr196 residue in USP13 after DNA damage functions as an essential regulatory event, and plays a critical role in the resistance of cancer cells to chemotherapy by deubiquitinating RAP80, promoting recruitment of complexes, and eliciting a DDR ( xref ; xref ) ( xref )."
USP13 is ubiquitinated.
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7
Lipopolysaccharide affects USP13
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Lipopolysaccharide inhibits USP13.
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Lipopolysaccharide decreases the amount of USP13.
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Lipopolysaccharide ubiquitinates USP13.
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Lipopolysaccharide leads to the ubiquitination of USP13. 2 / 2
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Lipopolysaccharide activates USP13.
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Lipopolysaccharide activates USP13. 2 / 2
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"To investigate whether USP13 mediated the deubiquitination of cohesin subunits, we cotransfected 293T cells with expression vectors for His ubiquitin and Myc-USP13, purified ubiquitinated proteins by Ni-NTA affinity chromatography, and performed Western blot with antibodies to SMC3 and RAD21 (XREF_FIG A)."
reach
"Considering that loss of PTEN contributed to fibroblasts phenotypic changes and USP13 interacted with PTEN and functioned as a deubiquitylase in epithelial cells, we subsequently sought to determine whether USP13 deficiency is responsible for the low PTEN expression observed in IPF fibroblasts."
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
reach
"Expression of USP13 (but not the C345A mutant) in MDA-MB-231 cells, which led to upregulation of PTEN and downregulation of phospho-AKT and phospho-FOXO1/3 (XREF_FIG), significantly inhibited cell proliferation (XREF_FIG), colony formation on soft agar (XREF_FIG), lactate production (XREF_FIG), glucose uptake (XREF_FIG) and tumor growth (XREF_FIG), while knockdown of PTEN (XREF_SUPPLEMENTARY) rescued the proliferation of USP13 overexpressing MDA-MB-231 cells (XREF_FIG)."
reach
"Together with results showing USP13 is important for DDR and RAP80 localization at the sites of DNA damage, we hypothesized that RAP80 ubiquitination is inhibitory of its function, and deubiquitination of RAP80 by USP13 following DNA damage promotes RAP80 function in the DDR pathway."
"USP13, in turn, deubiquitinates RAP80 and promotes RAP80 recruitment and proper DDR."
sparser
"Interestingly, USP13 associates with gp78 to attenuate polyubiquitination of ubiquitin-like protein 4A (UBL4A), a part of the Bag6 complex that helps chaperone retrotranslocated ERAD substrates to the proteasome, thereby protecting the Bag6 complex from proteasomal degradation and maintaining an adequate ERAD pathway, highlighting the importance of the associated DUB activity during ERAD [ xref ]."
reach
"Because the accumulation of Bag6 * upon USP13 depletion is significantly reduced in cells co-depleted of USP13 and gp78 (XREF_FIG), we propose that USP13 is required to antagonize a promiscuous activity of gp78 towards Ubl4A, which would otherwise impair the function of the Bag6 complex by altering its interaction pattern and/or increasing its cleavage by a cellular protease."
reach
"The close functional interconnection between the central PI3K-III subunits and the DUBs is demonstrated by the interesting observation that knock-down of VPS34 and Beclin 1 causes instability of USP10 and USP13, which strongly indicates the existence of a regulatory feedback loop [XREF_BIBR]."
USP13 affects cell population proliferation
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USP13 inhibits cell population proliferation.
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USP13 inhibits cell population proliferation. 10 / 12
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"Next, we treated infected THP-1 cells with a cell-permeable potent autophagy inhibitor, spautin-1.58 Spautin-1 promotes the degradation of BECN1 by inhibiting 2 USPs (ubiquitin-specific peptidases), USP10 and USP13, which target BECN1.58 Spautin-1 treatment of infected cells significantly decreased E. chaffeensis proliferation (Fig. 3B)."
Modified USP13 inhibits cell population proliferation. 3 / 3
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USP13 activates cell population proliferation.
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USP13 activates cell population proliferation. 10 / 11
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"Two independent USP13 shRNAs (XREF_FIG) both markedly increased the proliferation (XREF_FIG) and anchorage independent growth (XREF_FIG) of SUM159 breast cancer cells, while restoration of PTEN (XREF_FIG) or expression of an RNAi resistant USP13 mutant (XREF_SUPPLEMENTARY) completely reversed the effect of USP13 shRNA (XREF_FIG)."
reach
"In contrast, USP5 which shares 80% sequence similarity with USP13, neither interacted with STING in an overexpression system nor inhibited cGAS and STING induced activation of IFN-beta promoter in reporter assays (XREF_FIG), indicating a specific interaction between USP13 and STING."
sparser
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-κB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13(AE) removed K27-linked ubiquitination of STING in cells or in vitro , and (iv) overexpression of USP13 specifically disrupted TBK1-STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
sparser
"Interestingly, USP13 associates with gp78 to attenuate polyubiquitination of ubiquitin-like protein 4A (UBL4A), a part of the Bag6 complex that helps chaperone retrotranslocated ERAD substrates to the proteasome, thereby protecting the Bag6 complex from proteasomal degradation and maintaining an adequate ERAD pathway, highlighting the importance of the associated DUB activity during ERAD [ xref ]."
reach
"A study by Liu et al. (Liu et al., 2011) has demonstrated that Spautin-1 is a potent small-molecule inhibitor of USP10 and USP13, and treatment with Spautin-1 inhibits the deubiquitinase activity of USP10 and USP13, resulting in an increasing ubiquitination and accelerating degradation of Beclin1 in Vps34 complexes, ultimately inhibiting autophagy."
Spautin-1 activates USP13.
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Spautin-1 decreases the amount of USP13.
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1
reach
"Although no structural information for USP13 and USP10 is currently available, the enhanced DUB activity when USP13 interacts with USP10 or when they interact with Beclin1 suggest that the interaction of USP13 and USP10 with each other or with their substrates can lead to changes in their conformation which may be critical for the catalytic activities."
sparser
"Although no structural information for USP13 and USP10 is currently available, the enhanced DUB activity when USP13 interacts with USP10 or when they interact with Beclin1 suggest that the interaction of USP13 and USP10 with each other or with their substrates can lead to changes in their conformation which may be critical for the catalytic activities."
sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
reach
"It will be interesting to elucidate if the stability of the other PI3K and III complex members is also affected, as in the case of Spautin-1 -- mediated inhibition of USP10 and USP13 [XREF_BIBR] and if the control of Beclin 1 stability is mediated by HSP90 in general or whether this represents a regulatory event specifically developed in phagocytic cells."
sparser
"However, correlation analysis of RNA sequencing data from TCGA failed to provide evidence that USP13 and MCL1 were associated with each other at the messenger RNA (mRNA) level (Supplementary Fig. xref ), implying that USP13-mediated regulation of MCL1, if any, might not occur through a transcriptional mechanism."
sparser
"The isopeptidase‐independent mechanism of action proposed so far for USP13 relies on its UBA domains, which bind to ubiquitinated substrates, possibly inducing structural changes that stabilize them. xref Coincidentally, K63‐linked ubiquitin chains are required for EGFR sorting and degradation. xref This type of chains has also been reported as the preferred substrates for the USP13 UBA domains. xref We found that the UBA domains of USP13 were required for the binding to and stabilizing EGFR, as mutated UBA domains in USP13 resulted in a loss of USP13‐EGFR interaction and of EGFR stabilization."
"USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
reach
"Taken together, these studies suggest that USP14 is involved in the occurrence and progression of multiple malignant tumors.Other USP family members: USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
reach
"In contrast, USP5 which shares 80% sequence similarity with USP13, neither interacted with STING in an overexpression system nor inhibited cGAS and STING induced activation of IFN-beta promoter in reporter assays (XREF_FIG), indicating a specific interaction between USP13 and STING."
sparser
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-κB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13(AE) removed K27-linked ubiquitination of STING in cells or in vitro , and (iv) overexpression of USP13 specifically disrupted TBK1-STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
sparser
"To investigate whether USP13 mediated the deubiquitination of cohesin subunits, we cotransfected 293T cells with expression vectors for His-ubiquitin and Myc-USP13, purified ubiquitinated proteins by Ni-NTA affinity chromatography, and performed Western blot with antibodies to SMC3 and RAD21 ( xref A )."
reach
"Taken together, these studies suggest that USP14 is involved in the occurrence and progression of multiple malignant tumors.Other USP family members: USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
"USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
reach
"Although no structural information for USP13 and USP10 is currently available, the enhanced DUB activity when USP13 interacts with USP10 or when they interact with Beclin1 suggest that the interaction of USP13 and USP10 with each other or with their substrates can lead to changes in their conformation which may be critical for the catalytic activities."
sparser
"Although no structural information for USP13 and USP10 is currently available, the enhanced DUB activity when USP13 interacts with USP10 or when they interact with Beclin1 suggest that the interaction of USP13 and USP10 with each other or with their substrates can lead to changes in their conformation which may be critical for the catalytic activities."
sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
sparser
"We demonstrated that (1) a recurrent Q607R somatic substitution in CLK3 was identified in 8% of 100 human CCAs, particularly in patients with CCA metastasis; (2) the expression of CLK3 was significantly up-regulated in CCA compared with matched control tissues; (3) CLK3 knockdown significantly inhibited CCA aggressiveness in vitro and in vivo; (4) gene ontology term enrichment and MS assays indicated that high CLK3 expression in CCA patients mainly regulated nucleotide metabolism, especially purine biosynthesis; (5) mechanistically, CLK3 directly phosphorylated USP13 at Y708, which promoted its binding to c-Myc, a critical purine synthesis–associated transcription factor, thereby preventing Fbxl14-mediated c-Myc ubiquitination and activating the transcription of purine metabolic genes; (6) the CCA-associated CLK3-Q607R mutant induced USP13-Y708 phosphorylation and enhanced the activity of c-Myc; (7) in turn, c-Myc transcriptionally up-regulated CLK3; (8) importantly, levels of CLK3 significantly correlated with the expression of phospho-USP13-Y708, c-Myc, and ATIC in human CCA specimens; and (9) tacrine hydrochloride was identified as a potential compound to inhibit the aberrant CLK3-enhanced CCA invasiveness."
USP13 affects Neoplasm Invasiveness
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USP13 activates Neoplasm Invasiveness.
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USP13 inhibits Neoplasm Invasiveness.
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Spautin-1 decreases the amount of USP13.
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Spautin-1 activates USP13.
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reach
"Because the reductions in the levels of USP10 and USP13 in H4-LC3-GFP cells treated with spautin-1 appeared later than the reductions in the levels of Vps34 complexes and autophagy (XREF_FIG), the reduced levels of USP10 and USP13 are unlikely to be the primary reason for the ability of spautin-1 to reduce the levels of PtdIns3P and inhibit autophagy."
USP13 affects extracellular matrix
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USP13 increases the amount of extracellular matrix.
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USP13 activates extracellular matrix.
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reach
"Because the reductions in the levels of USP10 and USP13 in H4-LC3-GFP cells treated with spautin-1 appeared later than the reductions in the levels of Vps34 complexes and autophagy (XREF_FIG), the reduced levels of USP10 and USP13 are unlikely to be the primary reason for the ability of spautin-1 to reduce the levels of PtdIns3P and inhibit autophagy."
sparser
"The isopeptidase‐independent mechanism of action proposed so far for USP13 relies on its UBA domains, which bind to ubiquitinated substrates, possibly inducing structural changes that stabilize them. xref Coincidentally, K63‐linked ubiquitin chains are required for EGFR sorting and degradation. xref This type of chains has also been reported as the preferred substrates for the USP13 UBA domains. xref We found that the UBA domains of USP13 were required for the binding to and stabilizing EGFR, as mutated UBA domains in USP13 resulted in a loss of USP13‐EGFR interaction and of EGFR stabilization."
USP13 affects inflammatory response
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USP13 inhibits inflammatory response.
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USP13 activates inflammatory response.
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USP13 affects glycolytic process
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USP13 inhibits glycolytic process.
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USP13 activates glycolytic process.
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USP13 affects apoptotic process
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reach
"This overexpression upregulated PTEN protein and downregulated AKT and FOXO1/3 phosphorylation in the MDAMB-231 cell line (XREF_FIG) which expresses moderate but detectable levels of endogenous PTEN (XREF_SUPPLEMENTARY), while knockdown of PTEN in USP13 overexpressing MDA-MB-231 cells rescued the phosphorylation of both AKT and FOXO1/3 (XREF_SUPPLEMENTARY)."
sparser
"We observed that addition of His6-USP10, but not His6-USP13, reduced the amount of HA-Ub-conjugated FLAG-LC3B ( xref , C and D ), consistent with USP10 specifically catalyzing the deubiquitination of LC3B. Finally, we found that GFP-tagged LC3B (GFP-LC3B) co-immunoprecipitated with FLAG-USP10 but not FLAG-USP13 ( xref E )."
sparser
"We observed that addition of His6-USP10, but not His6-USP13, reduced the amount of HA-Ub-conjugated FLAG-LC3B ( xref , C and D ), consistent with USP10 specifically catalyzing the deubiquitination of LC3B. Finally, we found that GFP-tagged LC3B (GFP-LC3B) co-immunoprecipitated with FLAG-USP10 but not FLAG-USP13 ( xref E )."
reach
"Consistently, overexpression of wild type (WT), but not the catalytic-inactive (CA) mutant of USP13 with a mutation at the core enzymatic domain, could rescue the decreased nsp13 levels caused by USP13 depletion, suggesting that USP13 can regulate nsp13 levels most likely by deubiquitinating and consequently stabilizing nsp13."
USP13 activates USP13.
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USP13 decreases the amount of USP13.
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2
reach
"Moreover, treatment with a proteasome inhibitor blocked the c-Myc loss caused by USP13 knockdown (not depicted), but overexpression of USP13 delayed c-Myc turnover in the presence of cycloheximide (not depicted), suggesting a critical role of USP13 in preventing proteasomal degradation of c-Myc in GSCs."
sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
USP13 affects Neoplasm Metastasis
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USP13 affects Interferon
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USP13 affects GSC
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USP13 affects ERAD
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"Using an imaging-based screen, Liu et al. (2011) recently identified a highly potent small molecule inhibitor of autophagy they named spautin-1 (specific and potent autophagy inhibitor 1), which promotes degradation of the Vps34 complexes via inhibiting ubiquitin-specific processing protease 10 (USP10) and USP13, two ubiquitin-specific peptidases that target the deubiquitination of Beclin1.2."
reach
"The close functional interconnection between the central PI3K-III subunits and the DUBs is demonstrated by the interesting observation that knock-down of VPS34 and Beclin 1 causes instability of USP10 and USP13, which strongly indicates the existence of a regulatory feedback loop [XREF_BIBR]."
MiR-130b/301b affects USP13
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USP13 affects Carcinogenesis
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sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
Ubiquitin-proteasome affects USP13
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Ubiquitin-proteasome system affects USP13
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USP13 affects miR-301b-3p
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USP13 affects cell cycle
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USP13 activates cell cycle.
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USP13 activates cell cycle. 2 / 2
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"In addition, reconstitution of WT USP13, but not the T196A mutant, fully rescued the foci formation of the BRCA1-A complex, DNA repair and cell cycle checkpoint in USP13 deficient cells and reversed hypersensitivity to cisplatin or olaparib induced by USP13 deficiency (XREF_FIG and XREF_SUPPLEMENTARY)."
USP13 inhibits cell cycle.
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USP13 inhibits cell cycle. 1 / 1
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USP13 affects Proteasome
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USP13 activates Proteasome.
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USP13 inhibits Proteasome.
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USP13 inhibits Proteasome. 1 / 1
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USP13 affects Cell Survival
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USP13 affects Beclin1 subunit
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"We treated TBEV infected neuroblastoma cells with rapamycin (inducer of autophagy, as inhibition of mTOR mimics cellular starvation by blocking signals required for cell growth and proliferation), and spautin-1 (highly specific and potent autophagy inhibitor in mammalian cells, which promotes the degradation of Vps34 PI3 kinase complexes by inhibiting two ubiquitin specific peptidases, USP10 and USP13 that target the Beclin1 subunit of Vps34 complexes) and investigated the effect of the treatment of TBEV growth."
Spautin‐1 affects USP13
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Valproic acid affects USP13
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Polycyclic arene affects USP13
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Polycyclic arene increases the amount of USP13.
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Polycyclic arene decreases the amount of USP13.
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Phenylmercury acetate affects USP13
2
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Imidazolide affects USP13
|
1
1
Doxycycline affects USP13
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2
Benzo[a]pyrene affects USP13
2
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USP13 affects tumor growth
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2
USP13 affects stabilization TLR4
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2
USP13 affects stabilisation Mcl-1
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2
USP13 affects recruitment
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1
1
USP13 affects recruitment TBK1
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2
USP13 affects localization
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2
USP13 affects half-life MITF-M
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2
USP13 affects glioma stem cells
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2
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2
USP13 activates epithelial to mesenchymal transition. 2 / 2
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2
USP13 affects cell migration
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2
USP13 affects cell growth
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2
USP13 inhibits cell growth.
|
1
USP13 inhibits cell growth. 1 / 1
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1
USP13 activates cell growth.
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1
Mutated USP13 activates cell growth. 1 / 1
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1
USP13 affects cell death
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2
USP13 affects Virus Replication
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2
USP13 activates Virus Replication. 2 / 2
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2
eidos
"Our results demonstrate that USP13 is hijacked to maintain nsp13 expression and the inhibitory role of nsp13 in regulating type I IFN production , and USP13 inhibitor could be employed to suppress virus replication by targeting nsp13 for degradation thereby disrupting its inhibitory role in regulating type I IFN production ."
eidos
"Moreover , depletion of USP13 or treatment with USP13 inhibitor relieves the inhibitory role of nsp13 for type I IFN response and suppresses virus replication in host cells , suggesting that USP13 inhibitor could be employed to suppress virus replication by targeting nsp13 for degradation ."
USP13 affects UBL
|
2
USP13 affects TCRalpha
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2
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
USP13 affects MITF-M protein
|
2
USP13 affects FOXO1/3
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2
USP13 phosphorylates FOXO1/3.
|
1
USP13 dephosphorylates FOXO1/3.
|
1
reach
"This overexpression upregulated PTEN protein and downregulated AKT and FOXO1/3 phosphorylation in the MDAMB-231 cell line (XREF_FIG) which expresses moderate but detectable levels of endogenous PTEN (XREF_SUPPLEMENTARY), while knockdown of PTEN in USP13 overexpressing MDA-MB-231 cells rescued the phosphorylation of both AKT and FOXO1/3 (XREF_SUPPLEMENTARY)."
USP13 affects E3_Ub_ligase
|
2
USP13 affects 4-[4-[[2-(4-chlorophenyl)-5,5-dimethyl-1-cyclohexenyl]methyl]-1-piperazinyl]-N-[4-[[(2R)-4-(4-morpholinyl)-1-(phenylthio)butan-2-yl]amino]-3-(trifluoromethylsulfonyl)phenyl]sulfonylbenzamide
|
2
UBL affects USP13
|
2
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
Ubiquitin-like affects USP13
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1
Ubiquitin E3 affects USP13
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1
Trichloroethene affects USP13
1
|
Tetrachloromethane affects USP13
1
|
Tamibarotene affects USP13
1
|
Subsequent structural modification affects USP13
|
1
Spautin-1.58 Spautin-1 affects USP13
|
1
reach
"Next, we treated infected THP-1 cells with a cell-permeable potent autophagy inhibitor, spautin-1.58 Spautin-1 promotes the degradation of BECN1 by inhibiting 2 USPs (ubiquitin-specific peptidases), USP10 and USP13, which target BECN1.58 Spautin-1 treatment of infected cells significantly decreased E. chaffeensis proliferation (Fig. 3B)."
Reactive oxygen species affects USP13
|
1
Reactive oxygen species inhibits USP13. 1 / 1
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1
Pirinixic acid affects USP13
1
|
Nickel monoxide affects USP13
1
|
MiR-145-5p affects USP13
|
1
MiR-130b~301b affects USP13
|
1
Isobutanol affects USP13
1
|
Indometacin affects USP13
1
|
Imaging-based screening affects USP13
|
1
Hsa-miR-6080 affects USP13
1
|
Hsa-miR-548g-5p affects USP13
1
|
Hsa-miR-548f-5p affects USP13
1
|
Hsa-miR-548aj-5p affects USP13
1
|
Hsa-miR-539-3p affects USP13
1
|
Hsa-miR-4778-3p affects USP13
1
|
Hsa-miR-4659a-3p affects USP13
1
|
Hsa-miR-454-3p affects USP13
1
|
Hsa-miR-4295 affects USP13
1
|
Hsa-miR-3164 affects USP13
1
|
Hsa-miR-3163 affects USP13
1
|
Hsa-miR-3118 affects USP13
1
|
Hsa-miR-301b-3p affects USP13
1
|
Hsa-miR-1468-3p affects USP13
1
|
Hsa-miR-134-5p affects USP13
1
|
Hsa-miR-130b-3p affects USP13
1
|
Hsa-miR-1305 affects USP13
1
|
Formaldehyde affects USP13
1
|
Exposure LPS affects USP13
|
1
Endosulfan affects USP13
1
|
Copper atom affects USP13
1
|
Cefoperazone affects USP13
1
|
Bortezomib affects USP13
|
1
Bortezomib activates USP13. 1 / 1
|
1
Bisphenol A affects USP13
1
|
Autophagy inhibitor affects USP13
|
1
Autophagy inhibitor inhibits USP13. 1 / 1
|
1
Arsenic atom affects USP13
1
|
All-trans-retinoic acid affects USP13
1
|
Aflatoxin B1 affects USP13
1
|
Acrylamide affects USP13
1
|
Zoledronic Acid affects USP13
1
|
USP13 affects viruses caused nsp13 overexpression
|
1
USP13 affects virus-induced
|
1
USP13 affects ubiquitination nsp13
|
1
USP13 affects ubiquitination TXN
|
1
USP13 affects ubiquitinated nsp13
|
1
USP13 affects ubiquitinated Beclin1
|
1
USP13 affects ubiquitin-mediated mutant EGFR
|
1
USP13 affects ubiquitin-mediated TLR4
|
1
USP13 affects ubiquitin-like
|
1
USP13 affects ubiquitin-associated
|
1
USP13 inhibits ubiquitin-associated. 1 / 1
|
1
USP13 affects tumorigenic metastatic primary murine ovarian cancer cells
|
1
USP13 affects tumor initiation
|
1
USP13 affects synovial hyperplasia inflammatory cell infiltration cartilage bone collagen-induced arthritis
|
1
USP13 affects survival lung cancer cells treated afatinib
|
1
USP13 affects stability C adaptor CDH1
|
1
USP13 affects stability ACLY
|
1
USP13 affects signaling
|
1
USP13 affects sensitivity cervical cancer cells BH3 mimetic ABT-263
|
1
USP13 affects retention ac-SMC3 chromatin
|
1
USP13 affects replication stress response
|
1
USP13 affects reactive oxygen species
|
1
USP13 inhibits reactive oxygen species. 1 / 1
|
1
USP13 affects production
|
1
USP13 affects pathogenesis
|
1
USP13 activates pathogenesis. 1 / 1
|
1
USP13 affects p-RPA32 S33 staining
|
1
USP13 affects ovarian cancer cell
|
1
reach
"In addition, reconstitution of WT USP13, but not the T196A mutant, fully rescued the foci formation of the BRCA1-A complex, DNA repair and cell cycle checkpoint in USP13 deficient cells and reversed hypersensitivity to cisplatin or olaparib induced by USP13 deficiency (XREF_FIG and XREF_SUPPLEMENTARY)."
|
1
USP13 activates negative regulation of apoptotic process. 1 / 1
|
1
USP13 affects needs be determined
|
1
USP13 affects miR-130b-3p
|
1
USP13 affects membrane BAG6 cleavage
|
1
USP13 affects maturation
|
1
USP13 affects lung metastasis
|
1
USP13 affects lung inflammation
|
1
USP13 affects lung cancer cells
|
1
USP13 affects involvement development
|
1
USP13 affects increased lung inflammation enlargement alveolar spaces response CS exposure
|
1
USP13 affects hypoxia-induced activation TLR4 MyD88 NF-kappaB pathway
|
1
eidos
"Hypoxia Activates the TLR4 / MyD88 / NF-kappaB Pathway via Inducing USP13 in HCC Cells Since hypoxia has been recognized as an inducer of the activation of the TLR4 / MyD88 / NF-kappaB pathway in HCC ( Won et al ., 2015 ; Zhang et al ., 2016 ) , therefore , we aimed to investigate whether USP13 mediated the hypoxia-induced activation of the TLR4 / MyD88 / NF-kappaB pathway in HCC ."
USP13 affects hypersensitizes cells
|
1
USP13 affects half-life mutant protein NSCLC cells
|
1
USP13 affects growth metastasis mice
|
1
USP13 affects greater ubiquitinated nsp13
|
1
USP13 affects fumaric acid
|
1
USP13 inhibits fumaric acid. 1 / 1
|
1
USP13 affects fibronectin lung fibroblast cells
|
1
USP13 affects fast migrating BAG6 species
|
1
USP13 affects early autophagy
|
1
USP13 affects development metastasis high-grade serous ovarian carcinoma
|
1
USP13 affects development cervical cancer
|
1
USP13 affects deubiquitination ACLY
|
1
USP13 affects colony
|
1
USP13 affects cigarette smoke-induced alveolar space enlargement
|
1
USP13 affects cervical cancer cell
|
1
|
1
USP13 affects cell unstressed cells
|
1
USP13 affects cell cycle arrest
|
1
USP13 inhibits cell cycle arrest. 1 / 1
|
1
USP13 affects caused nsp13 overexpression
|
1
USP13 affects caspase activation
|
1
USP13 affects cancer cell chemoresistance
|
1
USP13 affects bind
|
1
USP13 affects autodegradation E3 ubiquitin ligase SIAH2
|
1
USP13 affects association
|
1
USP13 affects antiviral responses
|
1
USP13 affects active caspase
|
1
USP13 affects acetyl-CoA
|
1
USP13 activates acetyl-CoA. 1 / 1
|
1
USP13 affects accumulation ERAD substrates
|
1
USP13 affects abundance anti-apoptotic protein MCL1 lung
|
1
USP13 affects ZHX2 protein stability
|
1
USP13 affects Thr122
|
1
USP13 affects TXNIP lungs lung fibroblast cells
|
1
USP13 affects TNF-alpha induction
|
1
USP13 affects TLR4 abundance
|
1
USP13 affects TCRalpha-YFP
|
1
sparser
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-κB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13(AE) removed K27-linked ubiquitination of STING in cells or in vitro , and (iv) overexpression of USP13 specifically disrupted TBK1-STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
USP13 affects TAK1 phosphorylation
|
1
USP13 affects Stomach Neoplasms
|
1
USP13 deubiquitinates Stomach Neoplasms. 1 / 1
|
1
USP13 affects Smad4 half-life
|
1
USP13 affects Smad4 Protein
|
1
USP13 activates Smad4 Protein. 1 / 1
|
1
USP13 affects SiHa cells
|
1
USP13 affects STING-TBK1
|
1
reach
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-kappaB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13 (AE) removed K27 linked ubiquitination of STING in cells or in vitro, and (iv) overexpression of USP13 specifically disrupted TBK1 STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
USP13 affects QHO60603
1
|
|
1
USP13 affects PTEN-null
|
1
USP13 affects MuRF
|
1
USP13 affects MGC-803 cell migration
|
1
USP13 affects K63 polyubiquitination TRAF6
|
1
USP13 affects K48
|
1
USP13 affects IL-1R8
|
1
USP13 affects HMOX1 basal
|
1
USP13 affects HCC Cell Invasion Hep3B Huh7 cells expressed USP13 were transfected independent shRNAs USP13
|
1
USP13 affects GP78-mediated ubiquitination UBL4A
|
1
USP13 affects DNA Damage
|
1
USP13 inhibits DNA Damage. 1 / 1
|
1
USP13 affects Chk1 phosphorylation
|
1
USP13 affects CD3delta
|
1
USP13 affects BRCA1-A
|
1
reach
"In addition, reconstitution of WT USP13, but not the T196A mutant, fully rescued the foci formation of the BRCA1-A complex, DNA repair and cell cycle checkpoint in USP13 deficient cells and reversed hypersensitivity to cisplatin or olaparib induced by USP13 deficiency (XREF_FIG and XREF_SUPPLEMENTARY)."
USP13 affects BAG6 cleavage
|
1
USP13 affects B-Lymphocytes
|
1
USP13 activates B-Lymphocytes. 1 / 1
|
1
USP13 affects AKT inhibitors
|
1
USP13 inhibitor affects USP13
|
1
sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
USP-Y708F affects USP13
|
1
Thr122 affects USP13
|
1
sparser
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-κB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13(AE) removed K27-linked ubiquitination of STING in cells or in vitro , and (iv) overexpression of USP13 specifically disrupted TBK1-STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
Spautin-1 inhibitor affects USP13
|
1
sparser
"In support of this notion, we observed that (i) USP13 deficiency in mice or knockdown of USP13 in human cells potentiated HSV-1-triggered activation of IRF3 and NF-κB and subsequent induction of type I IFNs and proinflammatory cytokines, (ii) USP13 deficient cells restricted HSV-1 replication more profoundly than did the wild-type controls and USP13 deficient mice were more resistant to lethal HSV-1 infection compared to the wild-type littermates, (iii) USP13 but not USP13(AE) removed K27-linked ubiquitination of STING in cells or in vitro , and (iv) overexpression of USP13 specifically disrupted TBK1-STING association and knockdown or knockout of USP13 potentiated STING-TBK1 association after HSV-1 infection."
sparser
"The present study uncovers that USP10 is another critical DUB that deubiquitinates SKP2 and suppresses the ubiquitin-dependent proteasomal degradation of SKP2, which is compellingly supported by multiple lines of evidence: (1) our Co-IP experiments revealed compelling interaction of endogenous SKP2 with not only USP13 but also USP10 in KBM5-T315I and KBM5 cells (Fig. xref ); (2) the interaction of overexpressed SKP2 with overexpressed USP13 or USP10 was also confirmed in HEK293T cells but the USP10 missing the N-terminal 205 amino acid residues failed to bind to SKP2 (Fig. xref ); (3) overexpression of either USP13 or USP10 led to a higher SKP2 protein level and decreased p27 but overexpression of a DUB activity-disabled USP10 failed to do so (Fig. xref ); (4) shRNA-mediated knockdown or pharmacological inhibition of USP10 with Spautin1 remarkable decreased SKP2 and phosphorylated Bcr-Abl (but not total Bcr-Abl) but increased p27 in multiple CML cell lines (Fig. xref , Fig. xref ); (5) CHX chase assays showed that shortened the halflife of SKP2 protein (Fig. xref ); and (6) both pharmacological and genetic inhibition of USP10 could markedly increase K48-linked ubiquitinated SKP2 (Fig. xref )."
Reperfusion Injury affects USP13
|
1
Reperfusion Injury inhibits USP13. 1 / 1
|
1
RNA, Small Interfering affects USP13
|
1
RNA, Small Interfering inhibits USP13. 1 / 1
|
1
QHO60603 affects USP13
1
|
|
1
Phosphotransferases affects USP13
|
1
Phosphotransferases activates USP13. 1 / 1
|
1
Particulate Matter affects USP13
1
|
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
sparser
"USP7, a highly expressed DUB in prostate cancer and progressive multifocal leukoencephalopathy (PML), plays a direct role in PTEN deubiquitination and regulates its localization rather than protein stability. xref In addition, USP13 and OTUD3 can interact with PTEN and remove its polyubiquitin chain."
NF-kB p65 affects USP13
|
1
MuRF affects USP13
|
1
LPS with O-antigen affects USP13
|
1
LPS with O-antigen inhibits USP13. 1 / 1
|
1
K48 affects USP13
|
1
JNK inhibitor affects USP13
|
1
JNK depletion affects USP13
|
1
HPV oncogenes affects USP13
|
1
E3_Ub_ligase affects USP13
|
1
E3_Ub_ligase ubiquitinates USP13. 1 / 1
|
1
Central Nervous System affects USP13
|
1
Central Nervous System activates USP13. 1 / 1
|
1
BAG6 affects ubiquitin-like
|
1
3-isobutyl-1-methyl-7H-xanthine affects USP13
1
|
1-N-methyl-5-thiotetrazole affects USP13
1
|
(-)-epigallocatechin 3-gallate affects USP13
1
|