IndraLab
Statements
USP22 affects cell population proliferation
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USP22 activates cell population proliferation.
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USP22 activates cell population proliferation. 10 / 78
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"USP22 has been shown to promote the proliferation of human non small cell lung cancer cell H1129 and human bladder cancer cell EJ by facilitating cell cycle progression, which was supported by the observed G1 phase arrest and concomitant reduction in the S and G2/M phase when USP22 was depleted [XREF_BIBR, XREF_BIBR]."
USP22 inhibits cell population proliferation.
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"For instance, HULC can upregulate the expression of the ubiquitin specific peptidase 22 (USP22) protein by suppressing miR-6825-5p, miR-6845-5p, and miR-6886-3p at the epigenetic or transcriptional level in HCC cells; USP22 enhances the HULC induced deubiquitination of Sirt1 and stabilizes it, and Sirt1 stability induces the autophagy of HCC cells, thus increasing the resistance of HCC cells to oxaliplatin [XREF_BIBR]."
reach
"Given that SIRT1 is deubiquitinated by USP22 and stabilized at the protein level (Armour etal., 2013; Lin etal., 2012) and previous studies have reported that SIRT1 could negatively influence the chemosensitivity of HCC cells (Chen etal., 2012), our results supported the notion that USP22 increases SIRT1 protein levels in HCC cells."
reach
"Given that SIRT1 is deubiquitinated by USP22 and stabilized at the protein level (Armour etal., 2013; Lin etal., 2012) and previous studies have reported that SIRT1 could negatively influence the chemosensitivity of HCC cells (Chen etal., 2012), our results supported the notion that USP22 increases SIRT1 protein levels in HCC cells."
USP22 affects apoptotic process
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USP22 inhibits apoptotic process.
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USP22 activates apoptotic process.
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USP22 activates apoptotic process. 10 / 12
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"Silencing of USP22 in podocytes attenuated high d-glucose-induced apoptosis and inflammatory responses, evidenced by increases in proliferation and MMP levels and decreases in the apoptotic rate, ROS production, the Bax and Bcl -2 ratio, caspase-3 expression and secretion of TNF-alpha, IL-1beta, IL-6 and TGF-beta1."
Modified USP22 activates apoptotic process. 1 / 1
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USP22 affects Neoplasm Invasiveness
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USP22 activates Neoplasm Invasiveness.
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USP22 activates Neoplasm Invasiveness. 10 / 40
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USP22 activates Neoplasm Invasiveness. 2 / 2
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USP22 inhibits Neoplasm Invasiveness.
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"One important distinction is that previous findings are largely based on reporter assays analyzing USP22 mediated AR transactivation in Drosophila and human embryonic kidney (HEK) cells, and AR expression perturbation under conditions of ectopic overexpression of AR and USP22 in HEK cells."
eidos
"USP22 modulates both AR and MYC activity [ 8] , and USP22 mRNA expression was positively correlated with both AR and MYC mRNA expression ( p = 7.76e-14 and p =3 .36 e-7 , respectively ; Figure 1B ) , further supporting a pro-oncogenic role for USP22 in tumors with elevated AR and MYC expression ."
reach
"Together, these data demonstrate that USP22 regulates ligand independent AR residence at target gene loci and promotes AR driven CRPC gene profiles, which may have specificity for USP22 perturbation, further implicating USP22 as an independent effector of aggressive tumor phenotypes."
reach
"And correspondingly, overexpression of USP22 stabilized AR-V7 expression in a manner similar to USP14 (Fig. 5A–D), demonstrating that USP22 may also be involved in stabilizing the protein level of AR-V7, similar to USP14.In fact, the regulation of AR expression and function by USP22 in prostate cancer has been reported [37], but whether AR-V7 could be regulated by USP22 is elusive."
USP22 is modified
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USP22 is phosphorylated.
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USP22 is acetylated.
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"Furthermore, our data suggest that ATAC and SAGA control of gene transcription may be more specific than control of promoter H3K9 acetylation, indicating that specificity of transcriptional regulation by either complex may rely on unique effects of their additional enzymatic activities, namely H2B deubiquitination by USP22 and H4 acetylation by KAT14. xref Accordingly, our inspection of USP22 requirements in erythropoiesis suggest that they align with the stage specificity of SAGA but may exceed the effects of loss of SUPT20H and more directly resemble postcommitment contributions of KAT2A . Future studies investigating single and combined requirements of ATAC and SAGA enzymatic subunits in locus and cellular regulation will enhance our understanding of the transcriptional control of cell state and fate decisions, including in leukemia and the normal blood system."
USP22 is ubiquitinated.
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USP22 is deubiquitinated.
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USP22 affects cell cycle
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USP22 activates cell cycle.
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USP22 activates cell cycle. 10 / 25
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"Nevertheless, significant evidence is accumulating that indicates USP22 expression promotes cell cycle progression in certain cancer cell lines and that USP22 overexpression may enhance proliferation of cancer cells by facilitating premature transition through various cell cycle stages."
USP22 inhibits cell cycle.
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USP22 inhibits cell cycle. 10 / 15
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"Meanwhile, our flow cytometry analysis revealed that, compared with the control, USP22 shRNA transfected cells displayed a significantly higher portion of cells at the G0/G1 phases and significantly lower portions of cells at the S and G2/M phases (XREF_FIG C), indicating that USP22 silencing induces cell cycle arrest."
USP22 affects Neoplasm Metastasis
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USP22 activates Neoplasm Metastasis.
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USP22 inhibits Neoplasm Metastasis.
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"In addition, it has been shown that USP22 interacts with the c-Myc transcription factor in cancer cells ( xref ), and genetic c-Myc suppression impairs iNKT development but with increased PLZF expression ( xref ; xref ), raising the possibility that USP22 represses PLZF expression through its interaction with c-Myc."
sparser
"However, ChIP analysis failed detect USP22 binding to PLZF promoter DNA, together with the fact that USP22 interaction with c-Myc enhances but not suppresses c-Myc transcriptional activity ( xref ), largely excluding the possibility that USP22 inhibits PLZF transcription through c-Myc."
reach
"It could be through a direct mechanism where USP22 deubiquitylates c-MYC inducing its stabilization and activation, or indirectly through ubiquitin removal from histones at c-MYC target genes, recruitment of other transcriptional machinery or deubiquitylation of proteins important for c-MYC activity."
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USP22 activates epithelial to mesenchymal transition.
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USP22 activates epithelial to mesenchymal transition. 10 / 26
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"According to the results of previous studies, USP22 can induce EMT by regulating TGF-beta1 in lung cancer cells [XREF_BIBR], and elevated USP22 expression can promote EMT by up-regulating ZEB1 and Snail in pancreatic cancer cells though a process that involves focal adhesion kinase (FAK) signaling [XREF_BIBR]."
USP22 inhibits epithelial to mesenchymal transition.
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"Among them, the tumor-promoting effect of lncRNA KCNQ1OT1 is through the autocrine effect of tumor cell-derived exosomes, which mediates the miR-30a-5p/USP22 pathway to regulate the ubiquitination of PD-L1 and inhibits CD8+ T-cell response, thereby promoting CRC development (Figure 10)."
reach
"The tumor-promoting effect of lncRNA KCNQ1OT1 was through the autocrine effect of tumor cell-derived exosomes, which mediates the miR-30a-5p/USP22 pathway to regulate the ubiquitination of PD-L1 and inhibits CD8+ T-cell response, thereby promoting colorectal cancer development.Conclusion: Tumor cell-derived exosomes' KCNQ1OT1 could regulate PD-L1 ubiquitination through miR-30a-5p/USP22 to promote colorectal cancer immune escape."
reach
"Additionally, ubiquitin-specific peptidase 22 (USP22) in HCC [141], ubiquitin-specific peptidase 9, X-linked (USP9X) in OSCC [142], and ubiquitin C-terminal hydrolase L1 (UCHL1) in NSCLC [143] deubiquitinate and upregulate the PD-L1 expression.As a ubiquitously expressed protein, CMTM6 binds PD-L1 either at the plasma membrane or in recycling endosomes, repressing lysosome-mediated degradation of PD-L1 and upregulating protein half-time of PD-L1 without affecting the transcription level of PD-L1 [144, 145]."
reach
"Further, Pfam analysis of protein domain structures confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity (XREF_FIG and XREF_SUPPLEMENTARY)."
sparser
"The SAGA DUB module is highly conserved both in subunit composition and structural organization ( xref ; xref ; xref ; xref ; xref ; xref ), The deubiquitinating enzyme USP22 (Ubp8 in yeast) closely associates with two adapter proteins, ATXN7L3 and ENY2 (Sgf11 and Sus1 in yeast, respectively) ( xref ; xref ; xref ), and a fourth protein, ATXN7 (Sgf73), anchors the DUB module to the larger SAGA complex."
sparser
"It has been reported that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator Spt-Ada-Gcn5-acetyltransferase (SAGA) complex to regulate global levels of H2B monoubiquitination, thereby promoting antibody class switch recombination by facilitating nonhomologous end joining ( xref ; xref ; xref )."
sparser
"Further, Pfam analysis of protein domain structures ( xref ) confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity ( xref and xref ) ( xref )."
USP22 affects cell growth
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USP22 activates cell growth.
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USP22 inhibits cell growth.
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"To determine the potential clinical relevance of the USP22-FASN axis, we next assessed the expression of USP22 and FASN proteins in serial sections of 108 human CRC specimens, and found that FASN expression levels were significantly correlated with USP22 levels (Fig. xref , r = 0.6626, P < 0.0001)."
sparser
"Because p53 mutation usually loss the transcriptional activity and responses to upstream signals differently [ xref , xref ], p53-mediated repression of the USP22-FASN axis will be abolished in p53-mutated cancers, resulting in FASN stabilization, lipid accumulation, and tumor growth."
reach
"Further, Pfam analysis of protein domain structures confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity (XREF_FIG and XREF_SUPPLEMENTARY)."
sparser
"The SAGA DUB module is highly conserved both in subunit composition and structural organization ( xref ; xref ; xref ; xref ; xref ; xref ), The deubiquitinating enzyme USP22 (Ubp8 in yeast) closely associates with two adapter proteins, ATXN7L3 and ENY2 (Sgf11 and Sus1 in yeast, respectively) ( xref ; xref ; xref ), and a fourth protein, ATXN7 (Sgf73), anchors the DUB module to the larger SAGA complex."
sparser
"It has been reported that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator Spt-Ada-Gcn5-acetyltransferase (SAGA) complex to regulate global levels of H2B monoubiquitination, thereby promoting antibody class switch recombination by facilitating nonhomologous end joining ( xref ; xref ; xref )."
sparser
"Further, Pfam analysis of protein domain structures ( xref ) confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity ( xref and xref ) ( xref )."
USP22 affects Stomach Neoplasms
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USP22 activates Stomach Neoplasms.
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USP22 inhibits Stomach Neoplasms.
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"To further validate USP22 was modulating and stabilizing BRCA2 and PALB2 levels at the translational level, cells were depleted of USP22 again with and without treatment of the proteasome inhibitor MG132 to see if this could rescue PALB2 and BRCA2 levels in a USP22 knockdown background (Figure S1c)."
USP22 affects Histone_H2B
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USP22 deubiquitinates Histone_H2B.
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USP22 ubiquitinates Histone_H2B.
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"In addition, it has been shown that USP22 interacts with the c-Myc transcription factor in cancer cells ( xref ), and genetic c-Myc suppression impairs iNKT development but with increased PLZF expression ( xref ; xref ), raising the possibility that USP22 represses PLZF expression through its interaction with c-Myc."
sparser
"However, ChIP analysis failed detect USP22 binding to PLZF promoter DNA, together with the fact that USP22 interaction with c-Myc enhances but not suppresses c-Myc transcriptional activity ( xref ), largely excluding the possibility that USP22 inhibits PLZF transcription through c-Myc."
sparser
"Several studies demonstrated that USP22 silencing could activate p53. xref , xref Because USP22, Ube2d4, and Ube3b were important downstream genes of YWHAZ, we infer that YWHAZ downregulates p53 by activating USP22, Ube2d4, and Ube3b, which make P53 ubiquitination and lead to its proteasomal degradation."
reach
"Additionally, Usp22 directly deubiquitinates TRF1 (TBP (TATA box binding protein)-related factor 1) to regulate the transcription of cell cycle and apoptosis genes [XREF_BIBR] and inhibits the transcriptional activity of p53 by deubiquitinating SIRT1 histone deacetylase [XREF_BIBR] and by regulating MDMX stability [XREF_BIBR]."
eidos
"iv ) The downregulation of USP22 not only suppresses multidrug resistance-associated protein 1 ( MRP1 ) , enhances the intracellular accumulation of sorafenib , and finally inhibits cell proliferation and cancer angiogenesis , but also inhibits glycolysis in hepatocellular carcinoma ( HCC ) cells , enhancing sorafenib chemosensitivity and impairing cell metabolism ."
USP22 affects H2Bub1
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USP22 activates H2Bub1.
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USP22 deubiquitinates H2Bub1.
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USP22 inhibits H2Bub1.
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USP22 increases the amount of H2Bub1.
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"Similarly, Atanassov et al recently reported that depletion of USP22, a major H2B DUB, not only failed to increase H2Bub1 levels but even caused a mild decrease; this was ascribed to the fact that two newly identified H2B DUBs, USP27X and USP51, compete with USP22 for binding to the SAGA complex adaptor proteins ATXN7L3 and ENY2 XREF_BIBR."
sparser
"To determine the potential clinical relevance of the USP22-FASN axis, we next assessed the expression of USP22 and FASN proteins in serial sections of 108 human CRC specimens, and found that FASN expression levels were significantly correlated with USP22 levels (Fig. xref , r = 0.6626, P < 0.0001)."
sparser
"Because p53 mutation usually loss the transcriptional activity and responses to upstream signals differently [ xref , xref ], p53-mediated repression of the USP22-FASN axis will be abolished in p53-mutated cancers, resulting in FASN stabilization, lipid accumulation, and tumor growth."
reach
"As the Ubp8 ortholog USP22 was recently shown to interact with, deubiquitinate, and stabilize the Sir2 ortholog Sirt1, and conversely Sirt1 has been shown to mediate deacetylation of USP22 and the SAGA coactivator complex, the discovery of genetic and functional relationships between Sgf73, Ubp8, and Sir2 in yeast strongly suggests that mutant ataxin-7 protein could be impairing the function of not only Gcn5 in the context of the STAGA complex, but also USP22 in the deubiquitinase module."
sparser
"The SAGA DUB module is highly conserved both in subunit composition and structural organization ( xref ; xref ; xref ; xref ; xref ; xref ), The deubiquitinating enzyme USP22 (Ubp8 in yeast) closely associates with two adapter proteins, ATXN7L3 and ENY2 (Sgf11 and Sus1 in yeast, respectively) ( xref ; xref ; xref ), and a fourth protein, ATXN7 (Sgf73), anchors the DUB module to the larger SAGA complex."
sparser
"It has been reported that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator Spt-Ada-Gcn5-acetyltransferase (SAGA) complex to regulate global levels of H2B monoubiquitination, thereby promoting antibody class switch recombination by facilitating nonhomologous end joining ( xref ; xref ; xref )."
sparser
"Further, Pfam analysis of protein domain structures ( xref ) confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity ( xref and xref ) ( xref )."
reach
"Further, Pfam analysis of protein domain structures confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity (XREF_FIG and XREF_SUPPLEMENTARY)."
sparser
"To investigate the significance of USP22 and the 326 resulting STING-mediated upregulation of type III IFN and ISG signaling for viral327 defense, the role of the USP22-STING axis was tested during SARSexpression of STING, compared to wild-type (WT) and NHT 332 CRISPR/Cas9 control Caco-2 cells (Figure 6A)."
| DOI
sparser
"288 289 USP22 negatively regulates STING activation and ubiquitination 290 The differential response to ISD, but not poly(I:C), and the reversal of the IFN signature 291 in USP22-STING dKO hIECs suggests an important role of USP22 in the control of 292 STING-induced type III IFN signaling."
| DOI
"USP22 removes K27-linked ubiquitination on STING through cooperation with USP13"
reach
"288 289 USP22 negatively regulates STING activation and ubiquitination 290 The differential response to ISD, but not poly(I:C), and the reversal of the IFN signature 291 in USP22-STING dKO hIECs suggests an important role of USP22 in the control of 292 STING-induced type III IFN signaling."
| DOI
USP22 affects cell migration
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"Together with the observations that knockdown of KPNA2 impaired IRF3-USP22 associations after viral infection and that reconstitution of KPNA2 into USP22 knockout cells restored virus-induced nuclear translocation of IRF3 and expression of downstream genes, we concluded that USP22 promotes nuclear translocation of IRF3 primarily through deubiquitinating and stabilizing KPNA2."
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USP22 activates diphenylmethane-4,4'-diisocyanate.
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USP22 increases the amount of diphenylmethane-4,4'-diisocyanate.
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"Together with the observations that knockdown of KPNA2 impaired IRF3-USP22 associations after viral infection and that reconstitution of KPNA2 into USP22 knockout cells restored virus-induced nuclear translocation of IRF3 and expression of downstream genes, we concluded that USP22 promotes nuclear translocation of IRF3 primarily through deubiquitinating and stabilizing KPNA2."
USP22 affects cell differentiation
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USP22 inhibits cell differentiation.
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USP22 activates cell differentiation.
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"DUBs that have been reported to control developmental processes through deubiquitylating H2B include USP44, which represses genes involved in lineage commitment during mESC maintenance [XREF_BIBR], and USP22, which specifically inhibits expression of the pluripotency factor SOX2 during hESC differentiation [XREF_BIBR]."
sparser
"The SAGA DUB module is highly conserved both in subunit composition and structural organization ( xref ; xref ; xref ; xref ; xref ; xref ), The deubiquitinating enzyme USP22 (Ubp8 in yeast) closely associates with two adapter proteins, ATXN7L3 and ENY2 (Sgf11 and Sus1 in yeast, respectively) ( xref ; xref ; xref ), and a fourth protein, ATXN7 (Sgf73), anchors the DUB module to the larger SAGA complex."
sparser
"It has been reported that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator Spt-Ada-Gcn5-acetyltransferase (SAGA) complex to regulate global levels of H2B monoubiquitination, thereby promoting antibody class switch recombination by facilitating nonhomologous end joining ( xref ; xref ; xref )."
sparser
"Further, Pfam analysis of protein domain structures ( xref ) confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity ( xref and xref ) ( xref )."
reach
"Moreover, the study of the corresponding mechanism by which HULC upregulated COX-2 showed that HULC enhanced the level of ubiquitin specific peptidase 22 (USP22), which decreased ubiquitin mediated degradation of COX-2 protein by removing the conjugated polyubiquitin chains from COX-2 and finally stabilized COX2 protein."
reach
"In liver cancer, upregulation of lncRNA HULC activates autophagy by increasing the expression of ubiquitin specific peptidase 22 (USP22) which in turn prevents the ubiquitin mediated degradation of silent information regulator 1 (SIRT1) by removing the conjugated polyubiquitin chains from SIRT1."
reach
"It belongs to the DUB subset of Machado–Joseph disease (MJD) proteic domain-containing peptidases with Atxn3 (a.k.a. MJD1 and SCA3), encoded by the gene mutated in MJD, also termed type-3 spinocerebellar ataxia (SCA3), and Josephin domain-containing DUbs JosD1 and JosD2 (Table 1.7).27Aggregates formed by polyglutamine-expanded ataxin-7 sequester ubiquitin-specific peptidase USP22 that cannot then fulfill its deubiquitinating function in the SAGA complex, causing cytotoxicity and neurodegeneration [109]."
| PMC
sparser
"GCN5 is required for the association of SAGA with USP22, which is the component of its deubiquitination module, and the subsequent USP22-mediated deubiquitination of TRF1, which inhibits TRF1 degradation by proteasomes, thereby preventing signalling associated with telomere DNA damage and protecting telomeres from fusions."
USP22 affects Carcinogenesis
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USP22 activates Carcinogenesis.
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USP22 inhibits Carcinogenesis.
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USP22 inhibits Carcinogenesis. 1 / 2
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USP22 affects AR-V7
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USP22 binds AR-V7.
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"Unlike rutaecarpine, nobiletin failed to alter the GRP78-mediated degradation of AR-V7.In conclusion, this research not only demonstrates the reason why nobiletin suppressed the growth process of CRPC through the selective degradation of AR-V7, but also enriches our understanding of the degradation mechanism of AR-V7 and provides an efficient treatment target to overcome CRPC via targeting the interaction between AR-V7 and USP14/USP22 (Fig. 7G)."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
USP22 inhibits AR-V7.
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USP22 activates AR-V7.
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USP22 increases the amount of AR-V7.
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USP22 increases the amount of adenosine 5'-(pentahydrogen tetraphosphate).
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USP22 increases the amount of adenosine 5'-(pentahydrogen tetraphosphate). 6 / 6
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"The key findings of the study are as follows : (i) USP22 enhances CRC cell migration and invasion by inducing EMT, (ii) USP22 directly increases AP4 transcription to induce EMT and promote CRC cell metastasis to the lungs in vivo, and (iii) USP22 and AP4 overexpression is related to CRC progression and liver metastasis and poor outcomes in CRC patients."
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sparser
"To investigate the significance of USP22 and the 326 resulting STING-mediated upregulation of type III IFN and ISG signaling for viral327 defense, the role of the USP22-STING axis was tested during SARSexpression of STING, compared to wild-type (WT) and NHT 332 CRISPR/Cas9 control Caco-2 cells (Figure 6A)."
| DOI
sparser
"288 289 USP22 negatively regulates STING activation and ubiquitination 290 The differential response to ISD, but not poly(I:C), and the reversal of the IFN signature 291 in USP22-STING dKO hIECs suggests an important role of USP22 in the control of 292 STING-induced type III IFN signaling."
| DOI
reach
"In vitro assays showed that USP22 depletion suppressed ATC cell survival and proliferation by decreasing Rb phosphorylation and cyclin D2, inactivating Akt, and simultaneously upregulating Rb; USP22 silencing restrained cell migration and invasion by inhibiting epithelial-mesenchymal transition; USP22 knockdown promoted mitochondrion- mediated and caspase dependent apoptosis by upregulating Bax and Bid and promoting caspase-3 activation."
reach
"XREF_BIBR Similarly, HULC is able to stabilize silent information regulator 1 (Sirt1) protein in hepatocellular carcinoma cells because HULC can upregulate ubiquitin specific peptidase 22 (USP22), and suppress ubiquitin mediated degradation of Sirt1 protein by removing the conjugated polyubiquitin chains from Sirt1, XREF_BIBR leading to autophagy and chemoresistance."
reach
"The investigation for the corresponding mechanism by which HULC stabilized Sirt1 revealed that HULC upregulated ubiquitin specific peptidase 22 (USP22), leading to the decrease of ubiquitin mediated degradation of Sirt1 protein by removing the conjugated polyubiquitin chains from Sirt1."
HULC inhibits USP22.
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USP22 affects miR-34b
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USP22 affects inflammatory response
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USP22 activates inflammatory response.
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USP22 inhibits inflammatory response.
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USP22 affects Chromosomal Instability
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USP22 inhibits Chromosomal Instability. 6 / 6
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"Furthermore, two-sample Kolmogorov-Smirnov (KS) tests revealed statistically significant increases (siUSP22-2, siUSP22-3) and a decrease (siUSP22-Pool) in cumulative nuclear area frequency distributions relative to siControl (XREF_FIG D; Table S5) that are consistent with reduced USP22 expression inducing CIN."
reach
"In this regard, while USP22 has been proposed as a novel therapeutic target based on its oncogenic functions [XREF_BIBR, XREF_BIBR, XREF_BIBR], our work suggests that USP22 inhibition will induce CIN that may promote cancer progression and/or the development of secondary malignancies."
USP22 affects Cell Survival
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USP22 activates Cell Survival.
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USP22 inhibits Cell Survival.
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E3_Ub_ligase affects USP22
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MiR-4490 affects USP22
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USP22 affects transcription, DNA-templated
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USP22 activates transcription, DNA-templated. 5 / 5
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sparser
"At the biochemical level, these Polycomb proteins function as global transcriptional repressors by catalyzing the ubiquitylation of histone H2A. In yeast, the USP22 homolog functions as a transcriptional coactivator by removing ubiquitin from a distinct core histones, H2B. Given that USP22 is expressed in cancer as part of an 11 gene signature that includes transcriptional repressors which ubiquitylate H2A, it seemed possible that USP22 might activate transcription in part via the deubiquitylation of this same substrate."
USP22 affects immune response
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eidos
"After treatment with irradiation , XPC foci were significantly increased in LN-USP22hi and C42-USP22hi cells as well as decreased in LN-shUSP22 and C42-shUSP22 compared to corresponding controls ( Figure 5G ) , suggesting that USP22 modulates XPC activity basally and in response to genotoxic insult ."
eidos
"USP22 induced deubiquitylation of XPC without an increase of the protein half-life ( Supplemental Figure 5A ) , suggesting the alternative hypothesis that USP22 may modulate XPC activity through de-polyubiquitylation , as XPC is known to be polyubiquitylated to promote efficient DNA repair [ 32,33,39 ] ."
USP22 affects NSCLC
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USP22 affects LINC01426
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"In our study, we found that knockout of USP22 impaired virus-triggered nuclear translocation of p65 and induction of p65-target genes such as Tnf and Il6 , which was restored by reconstitution of KPNA2, suggesting a role of the USP22–KPNA2 axis in NF-κB activation after viral infection (data not shown)."
sparser
"Our findings in lung adenocarcinoma cell line (Figure xref ) and xenografts (Figure xref ) support that USP22 could promote the phosphorylation of histone H2AX via deubiquitinating histone H2A, thus contributing to the DNA damage repair induced by cisplatin and leading to cisplatin resistance."
reach
"To further validate USP22 was modulating and stabilizing BRCA2 and PALB2 levels at the translational level, cells were depleted of USP22 again with and without treatment of the proteasome inhibitor MG132 to see if this could rescue PALB2 and BRCA2 levels in a USP22 knockdown background (Figure S1c)."
LINC01426 affects USP22
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Gal-SLPs affects USP22
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Gal-SLPs inhibits USP22.
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Gal-SLPs decreases the amount of USP22.
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MiR-34b affects USP22
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MiR-30e-5p affects USP22
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USP22 affects miR-132-3p
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USP22 affects glycolytic process
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USP22 activates glycolytic process. 4 / 4
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eidos
"In particular , Gal-SLPs can induce a trio synergetic effect : i ) sorafenib elevated intracellular levels of ROS , which oxidize B-PDEAEA to trigger rapid shUSP22 release for efficient gene downregulation ; ii ) the downregulation of USP22 led to downregulation of multidrug resistance-associated protein 1 ( MRP1 ) and inhibition of glycolysis , dramatically impairing MDR and achieving higher intracellular sorafenib accumulation , thus generating an ROS-responsive positive feedback loop ; iii ) the downregulation of USP22 suppressed the cell metabolism of cancer cells and further influenced cancer stemness ."
USP22 affects cell death
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1
2
USP22 activates cell death.
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1
1
USP22 inhibits cell death.
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1
USP22 inhibits cell death. 1 / 1
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1
reach
"Moreover, USP22, SIRT1, or SLC7A11 elevation contributed to enhanced cardiomyocyte viability and attenuated ferroptosis induced cell death in vitro, accompanied by increased GSH levels, as well as decreased reactive oxygen species production, lipid peroxidation, and iron accumulation."
USP22 affects Wnt/β-catenin
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4
reach
"211 212 USP22 negatively regulates STAT1 signaling and IFN-λ1 expression 213 The expression of ISGs is typically induced upon activation of IFN signaling pathways 214 during pathogen invasion or autoinflammatory disease and serves to control 215 inflammation and other defensive mechanisms 9 ."
| DOI
reach
"Other inflammatory mediators secreted by PDA cells include granulocyte colony-stimulating factor (G-CSF) (41), IL-6 (42), IL-1α (43), IL-1β (44, 45), ubiquitin specific peptidase 22 (USP22) (46), C-X-C motif chemokine ligand 8 (CXCL8) (47), matrix metallopeptidase 9 (MMP-9) and indoleamine-2,3-dioxygenase (IDO) (48), which all contribute to the establishment of immunosuppressive TME in pancreatic cancer (
Figure 1
)."
USP22 affects AP4
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4
sparser
"Additionally, assessment of CRC clinicopathological characteristics demonstrated that USP22 and AP4 expression levels were significantly associated with pT classification, pM classification, AJCC stage and tumor markers used as prognostic indicators of postoperative recurrence and metastasis in CRC, including CEA and CA199."
AP4 affects USP22
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4
sparser
"Additionally, assessment of CRC clinicopathological characteristics demonstrated that USP22 and AP4 expression levels were significantly associated with pT classification, pM classification, AJCC stage and tumor markers used as prognostic indicators of postoperative recurrence and metastasis in CRC, including CEA and CA199."
Valproic acid affects USP22
3
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Valproic acid decreases the amount of USP22.
2
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Valproic acid methylates USP22.
1
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MiR-30-5p affects USP22
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3
USP22 affects homologous recombination
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3
USP22 affects cellular survival
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3
eidos
"The USP22-sensitive ubiquitylome reveals altered modification of DNA repair-related proteins The USP22-sensitive transcriptome implicated USP22 in affecting DDR-related pathways ( Figure 2 ) , and in vitro and in vivo studies demonstrated that USP22 modulates proliferative phenotypes as well as cellular survival ( Figures 2-3 ) ."
eidos
"Moreover , USP22 depletion decreased cellular survival in response to cisplatin at 2.5 muM ( 1.9-fold ; p =0 .004 ) and 5 muM ( 3.5-fold ; p =0 .0002 ) in CRPC cells ( Figure 2E , right ) as well as HT-sensitive cells ( p =0 .001 ; Supplemental Figure 2E , right ) , indicating that USP22 is required for cellular survival after DNA damage ."
USP22 affects cell stemness
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3
USP22 affects c-NHEJ
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3
USP22 affects angiogenesis
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1
2
reach
"Unlike rutaecarpine, nobiletin failed to alter the GRP78-mediated degradation of AR-V7.In conclusion, this research not only demonstrates the reason why nobiletin suppressed the growth process of CRPC through the selective degradation of AR-V7, but also enriches our understanding of the degradation mechanism of AR-V7 and provides an efficient treatment target to overcome CRPC via targeting the interaction between AR-V7 and USP14/USP22 (Fig. 7G)."
reach
"However, it is worth noting that nobiletin had no effect on the interactions between AR-FL and USP14/USP22, which may explain why nobiletin has a certain selectivity in inducing the degradation of AR-V7.Our previous study has been demonstrated that rutaecarpinecan selectively trigger the GRP78-dependent AR-V7 degradation [23]."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
USP22 affects Sirt1/JAK/STAT3
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3
USP22 affects Osteosarcoma
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1
1
USP22 affects OS tumor growth
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3
USP22 affects MED1
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3
sparser
"The interaction between the endogenous USP22 and MED1 was further validated in mouse primary iNKT cells because MED1 was detected in anti-USP22 immunoprecipitates but not the normal rabbit IgG controls ( xref ), indicating a possibility that USP22 regulates iNKT cell development through, at least partially, MED1 interaction."
USP22 affects LUAD
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3
USP22 affects H2Aub
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3
USP22 affects DNA Damage
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3
USP22 affects Carcinoma, Non-Small-Cell Lung
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1
USP22 activates Carcinoma, Non-Small-Cell Lung. 1 / 3
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1
USP22 affects AR-FL
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3
reach
"However, it is worth noting that nobiletin had no effect on the interactions between AR-FL and USP14/USP22, which may explain why nobiletin has a certain selectivity in inducing the degradation of AR-V7.Our previous study has been demonstrated that rutaecarpinecan selectively trigger the GRP78-dependent AR-V7 degradation [23]."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
reach
"Unlike rutaecarpine, nobiletin failed to alter the GRP78-mediated degradation of AR-V7.In conclusion, this research not only demonstrates the reason why nobiletin suppressed the growth process of CRPC through the selective degradation of AR-V7, but also enriches our understanding of the degradation mechanism of AR-V7 and provides an efficient treatment target to overcome CRPC via targeting the interaction between AR-V7 and USP14/USP22 (Fig. 7G)."
reach
"However, it is worth noting that nobiletin had no effect on the interactions between AR-FL and USP14/USP22, which may explain why nobiletin has a certain selectivity in inducing the degradation of AR-V7.Our previous study has been demonstrated that rutaecarpinecan selectively trigger the GRP78-dependent AR-V7 degradation [23]."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
MED1 affects USP22
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3
sparser
"The interaction between the endogenous USP22 and MED1 was further validated in mouse primary iNKT cells because MED1 was detected in anti-USP22 immunoprecipitates but not the normal rabbit IgG controls ( xref ), indicating a possibility that USP22 regulates iNKT cell development through, at least partially, MED1 interaction."
sparser
"In our study, we found that knockout of USP22 impaired virus-triggered nuclear translocation of p65 and induction of p65-target genes such as Tnf and Il6 , which was restored by reconstitution of KPNA2, suggesting a role of the USP22–KPNA2 axis in NF-κB activation after viral infection (data not shown)."
AR-V7 affects USP22
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3
reach
"Unlike rutaecarpine, nobiletin failed to alter the GRP78-mediated degradation of AR-V7.In conclusion, this research not only demonstrates the reason why nobiletin suppressed the growth process of CRPC through the selective degradation of AR-V7, but also enriches our understanding of the degradation mechanism of AR-V7 and provides an efficient treatment target to overcome CRPC via targeting the interaction between AR-V7 and USP14/USP22 (Fig. 7G)."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
AR-FL affects USP22
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3
reach
"However, it is worth noting that nobiletin had no effect on the interactions between AR-FL and USP14/USP22, which may explain why nobiletin has a certain selectivity in inducing the degradation of AR-V7.Our previous study has been demonstrated that rutaecarpinecan selectively trigger the GRP78-dependent AR-V7 degradation [23]."
reach
"Immunofluorescence and western blot experiments showed that these molecular events mainly occurred in the nucleus.We also confirmed that nobiletin can significantly decrease the interactions between AR-V7 and USP14/USP22 in a time and concentration-dependent manner, but did not affect the interactions between AR-FL and USP14/USP22, which may explain why nobiletin exhibits a certain selectivity in inducing the degradation of AR-V7."
5-formyluracil affects USP22
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3
5-formyluracil activates USP22. 3 / 3
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3
reach
"After the mice injected with Bel/Fu cells with siRNA interference of USP22 expression were treated with 5-FU, the size of the subcutaneous xenografts significantly decreased, suggesting that downregulation of USP22 expression mitigated 5-FU resistance and increased the sensitivity of HCC to chemotherapy drugs, which may be related to the physiological function of USP22 to form a complex with BMI1."
reach
"After the Bel/Fu cells were injected into nude mice, the mean diameter of the subcutaneous xenografts that developed was 1.5 cm, whereas for mice injected with Bel/Fu cells with stable expression of USP22 siRNA, the mean diameter was smaller (1.4 cm, n = 6, P < 0.05, XREF_FIG); after the mice injected with Bel/Fu cells were treated with 5-FU, the mean diameter of xenografts was smaller (1.2 cm, n = 6, P < 0.05, XREF_FIG); after the mice injected with Bel/Fu cells with stable expression of USP22 siRNA were treated with 5-FU, the mean diameter of xenografts was 0.9 cm, significantly smaller than that observed in mice injected with Bel/Fu cells alone (n = 6, P < 0.05, XREF_FIG)."
Reactive oxygen species affects USP22
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2
Hsa-miR-6825-5p affects USP22
2
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CircFAT1 affects USP22
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2
USP22 affects ubH2B
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2
USP22 affects tumor growth
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1
USP22 affects sensitivity PC cells cisplatin
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2
USP22 affects repair
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2
USP22 affects proteolysis
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2
USP22 inhibits proteolysis.
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1
USP22 inhibits proteolysis. 1 / 1
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1
USP22 activates proteolysis.
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1
USP22 activates proteolysis. 1 / 1
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1
USP22 affects pathway
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2
USP22 affects melanoma BRAF resistance
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2
USP22 affects hSAGA
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2
USP22 affects growth
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2
USP22 affects ferroptosis-induced myocardial cell death
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2
USP22 affects fatty acid biosynthetic process
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2
USP22 affects cell cycle phase transition
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2
USP22 affects cell cycle arrest
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2
USP22 affects cell apoptosis
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1
USP22 affects UBC
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2
USP22 affects OS cell
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2
USP22 affects NLRP3 inflammasome
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2
USP22 affects IFN-λ1
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2
USP22 affects H2BK120ub
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2
USP22 affects GC
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2
USP22 affects Drug Resistance, Multiple
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2
USP22 activates Drug Resistance, Multiple. 2 / 2
|
2
eidos
"Our previous research showed that ubiquitin specific peptidase 22 ( USP22 ) induces multidrug resistance of HCC via the Sirtuin 1 ( SIRT1 ) / AKT / multidrug resistance associated protein 1 ( MRP1 ) signaling pathway151 ; and recently we also explored the relationship among USP22 , sorafenib resistance , and cancer stemness.152 Precision therapy is the future direction of cancer treatment ."
USP22 affects DSB repair
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2
USP22 affects DNA repair
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2
USP22 affects CRPC
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2
USP22 affects AR-V7 protein
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2
USP22 affects ADR
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2
USP22 affects 5-formyluracil
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2
USP22 inhibits 5-formyluracil. 2 / 2
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2
Atx7 affects USP22
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2
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2
Streptozocin affects USP22
1
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Sphingosine-1-phosphocholine affects USP22
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1
Sphingosine-1-phosphocholine activates USP22. 1 / 1
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1
reach
"USP 22, KDM3A, and YAP1 were found to be down-regulated in MI/RI and SPC protected MI/RI rats, as evidenced by up-regulated expressions of USP22, KDM3A, and YAP1, reduced pathological injury in the myocardium, myocardial infarction areas, apoptosis, and levels of CK-MB, cTnI, and LDH, and enhanced H9c2 cell viability; while the protective effects of Sevo were counteracted by silencing of USP22, KDM3A, and SPC upregulated USP22, which stabilized KDM3A protein levels via deubiquitination, and KDM3A inhibited histone 3 lysine 9 di-methylation (H3K9me2) levels in the YAP1 promoter to encourage YAP1 transcription, to reduce MI/RI."
Small hairpin RNA affects USP22
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1
Released shUSP22 affects USP22
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1
Reconstitution PAM-mutated WT mutant USP22 cells affects USP22
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1
Pirinixic acid affects USP22
1
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Near % affects USP22
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1
MiRNA-329-3p affects USP22
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1
MiR-6886-3p affects USP22
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1
MiR-144-3p affects USP22
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1
Infection lentivirus UPS22-specifc shRNA affects USP22
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1
Hsa-miR-6893-5p affects USP22
1
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Hsa-miR-6876-5p affects USP22
1
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Hsa-miR-6782-5p affects USP22
1
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Hsa-miR-637 affects USP22
1
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Hsa-miR-485-5p affects USP22
1
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Hsa-miR-483-3p affects USP22
1
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Hsa-miR-4728-5p affects USP22
1
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Hsa-miR-4524b-3p affects USP22
1
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Hsa-miR-4433b-3p affects USP22
1
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Hsa-miR-4252 affects USP22
1
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Hsa-miR-3926 affects USP22
1
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Hsa-miR-3680-5p affects USP22
1
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Hsa-miR-3612 affects USP22
1
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Hsa-miR-328-5p affects USP22
1
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Hsa-miR-3179 affects USP22
1
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Hsa-miR-3154 affects USP22
1
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Hsa-miR-29c-5p affects USP22
1
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Hsa-miR-183-5p affects USP22
1
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Hsa-miR-127-5p affects USP22
1
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Foci affects USP22
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1
Anthracycline affects USP22
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1
Anthracycline decreases the amount of USP22. 1 / 1
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1
USP27X affects USP22
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1
USP22 affects transcriptional regulator
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1
USP22 leads to the ubiquitination of transcriptional regulator. 1 / 1
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1
USP22 affects stemness features cells
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1
USP22 affects stem cell markers
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1
USP22 affects sorafenib chemosensitivity
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1
eidos
"iv ) The downregulation of USP22 not only suppresses multidrug resistance-associated protein 1 ( MRP1 ) , enhances the intracellular accumulation of sorafenib , and finally inhibits cell proliferation and cancer angiogenesis , but also inhibits glycolysis in hepatocellular carcinoma ( HCC ) cells , enhancing sorafenib chemosensitivity and impairing cell metabolism ."
USP22 affects response DNA
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1
USP22 affects protein p-PI3K
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1
USP22 affects pro-inflammatory responses aeruginosa-induced keratitis
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1
USP22 affects pathways
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1
USP22 affects neurogenesis
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1
USP22 activates neurogenesis. 1 / 1
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1
USP22 affects miR-30-5p
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1
USP22 affects miR-144-3p
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1
USP22 affects memory capacity
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1
USP22 affects isotype switching
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1
USP22 activates isotype switching. 1 / 1
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1
USP22 affects histone H2A ubiquitination
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1
USP22 inhibits histone H2A ubiquitination. 1 / 1
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1
USP22 affects growth metastasis cells
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1
USP22 affects ganetespib
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1
USP22 inhibits ganetespib. 1 / 1
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1
USP22 affects function caused KCNQ1OT1
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1
USP22 affects foci
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1
USP22 affects fluthiacet-methyl
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1
USP22 activates fluthiacet-methyl. 1 / 1
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1
USP22 affects deubiquitylation histones H2A
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1
USP22 affects desiccated thyroid extract
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1
USP22 activates desiccated thyroid extract. 1 / 1
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1
USP22 affects critical step
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1
USP22 affects cl-caspase 3
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1
USP22 affects cerebral R-induced oxidative stress
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1
USP22 affects beta-catenin nuclear localisation
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1
USP22 affects antiviral response cytoplasm
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1
USP22 affects XPC function
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1
USP22 affects TRF1 deubiquitylation
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1
USP22 affects SPT3/TAF9/GCN5
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1
USP22 affects SOS1/RAS/ERK
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1
USP22 affects SIRT1 stability
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1
USP22 affects SIRT-1
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1
USP22 affects SAGA complex
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1
sparser
"Looking more broadly across the genome, we found that sites that significantly gained H2BK120Ub in both Usp22KO and Usp22-RNP targeted Tregs were enriched for activating histone modifications (H3K4me3, H3K4me and H3K27ac) suggesting that changes occurred at gene regulatory elements, including at Treg-specific super enhancers ( xref , xref )."
reach
"Additionally, DHT stimulation in USP22 upregulated cells promoted a ~ 4-fold increase in ODC expression above DHT stimulated conditions (XREF_FIG), which was significantly sustained in LN-USP22 cells upon Casodex treatment (although compared to the AR targets examined in XREF_FIG, Casodex showed a relatively more pronounced inhibitory effect)."
USP22 affects Neoplastic Stem Cells
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1
USP22 activates Neoplastic Stem Cells. 1 / 1
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1
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1
USP22 inhibits NLRP3 inflammasome complex assembly. 1 / 1
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1
reach
"Other inflammatory mediators secreted by PDA cells include granulocyte colony-stimulating factor (G-CSF) (41), IL-6 (42), IL-1α (43), IL-1β (44, 45), ubiquitin specific peptidase 22 (USP22) (46), C-X-C motif chemokine ligand 8 (CXCL8) (47), matrix metallopeptidase 9 (MMP-9) and indoleamine-2,3-dioxygenase (IDO) (48), which all contribute to the establishment of immunosuppressive TME in pancreatic cancer (
Figure 1
)."
USP22 affects IL-1α
|
1
reach
"Other inflammatory mediators secreted by PDA cells include granulocyte colony-stimulating factor (G-CSF) (41), IL-6 (42), IL-1α (43), IL-1β (44, 45), ubiquitin specific peptidase 22 (USP22) (46), C-X-C motif chemokine ligand 8 (CXCL8) (47), matrix metallopeptidase 9 (MMP-9) and indoleamine-2,3-dioxygenase (IDO) (48), which all contribute to the establishment of immunosuppressive TME in pancreatic cancer (
Figure 1
)."
USP22 affects HATs
|
1
USP22 affects Genomic Instability
|
1
USP22 inhibits Genomic Instability. 1 / 1
|
1
USP22 affects GSC
|
1
USP22 affects GC cell EMT-induced metastasis
|
1
USP22 affects FUSE)-binding protein 1
|
1
USP22 affects EMT process OS cells
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1
USP22 affects DUB module
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1
USP22 affects CRPC-associated gene profile
|
1
USP22 affects AKT/GSK-3/Cyclin
|
1
SPT3/TAF9/GCN5 affects USP22
|
1
SNHG16 knockdown affects USP22
|
1
SIRT-1 affects USP22
|
1
sparser
"Looking more broadly across the genome, we found that sites that significantly gained H2BK120Ub in both Usp22KO and Usp22-RNP targeted Tregs were enriched for activating histone modifications (H3K4me3, H3K4me and H3K27ac) suggesting that changes occurred at gene regulatory elements, including at Treg-specific super enhancers ( xref , xref )."
MiR-6825-5p affects USP22
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1
HATs affects USP22
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1
Dietary Fats affects USP22
1
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DUB module affects USP22
|
1
APCCDC20 affects USP22
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1
17alpha-ethynylestradiol affects USP22
1
|