IndraLab

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USP22 binds SIRT1. 41 / 61
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"SIRT1 physically interacts with USP22 as a mediator of USP22."
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"USP22 can also form a complex with the histone deacetylase SIRT1, which serves a similar repressive action on Sox2."
25206361
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"Moreover, USP22 directly interacts with sirtuin 1 (SIRT1) and positively regulates SIRT1 protein expression, leading to activation of the SIRT1/AKT/ABCC1 pathway and MDR of hepatocellular carcinoma [ xref ]."
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"Sgf73 can also physically interact with Sir2 and Ubp8, a finding replicated in mammals by interaction of USP22 with human SIRT1 ( xref ; xref ), suggesting that altered chromatin-modifying activities in the central nervous system may contribute to SCA7 neurodegeneration."
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"These results indicate that USP22 directly interacts with SIRT1 and contributes to stabilization of SIRT1 protein in FLT3-ITD AML cells."
25280219
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"We show that USP22 directly interacts with SIRT1 in FLT3-ITD AML cells in a FLT3-kinase-independent manner."
25280219
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"By using Co-immunoprecipitation, the interaction between USP22 and Sirt1 was validated in cells transfected with KLF3-AS1 overexpression plasmid or not (Fig.  xref E)."
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"USP22 Interacts with SIRT1 and Maintains Its Protein Expression."
25280219
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"These results indicate that USP22 directly interacts with SIRT1 and contributes to stabilization of SIRT1 protein in FLT3-ITD AML cells."
25280219
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"It has been demonstrated that USP22 interacts with Sirt1 and removes Sirt1 polyubiquitination to enhance its protein stability [14] ."
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"In addition, USP22 can directly interact with SIRT1 and regulate the protein expression level of SIRT1, which promotes the resistance of hepatoma cells to 5-fluorouracil (5-FU) ( xref )."
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"Consistently, MS and Co‐IP analysis verified the interaction between USP22 and SIRT1 (Figure  xref )."
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"USP22 can also form a complex with the histone deacetylase SIRT1, which serves a similar repressive action on Sox2."
25206361
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"Considering that USP22 typically functions through interactions with different proteins and regulates protein stability via deubiquitination, we utilized MS to investigate the binding partners of USP22 and revealed that USP22 interacts with SIRT1 and stabilizes SIRT1 expression through its deubiquitinase activity."
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"Functional association of USP22 with SIRT1 in vitro and in vivo."
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"Besides, the direct interaction of USP22 and Sirt1 was validated by co-immunoprecipitation, and the result was consistent with the precious study (Ma et al. xref )."
36627572
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"Studies have demonstrated that USP22 directly interacts with SIRT1, activating the AKT/GSK-3β/multidrug resistance-associated protein 1 (MRP1) pathway, thereby enhancing 5-Fu efflux and reducing 5-Fu-induced apoptosis in HCC cells [ xref ]."
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"In this study, USP22 directly interacted with SIRT1 and positively regulated SIRT1 protein expression."
28417539
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"USP22 directly interacts with SIRT1 based on the co-immunoprecipitation assay."
28417539
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"Meanwhile, the interaction between USP22 and SIRT1 was validated using a ChIP assay ( xref )."
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"Additionally, to better understand the role of USP22-SIRT1 axis in ferroptosis-induced cell death, the effects of overexpression or knockdown of SIRT1 on ferroptosis signaling pathway were examined using Western blot analysis ( xref )."
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"The zinc finger-containing N terminus of USP22 binds Sirt1."
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"USP22 interacts with and stabilizes SIRT1 by removing polyubiquitin chains conjugated onto SIRT1 in mouse embryonic development [XREF_BIBR]."
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"To test this hypothesis, we first determined whether endogenous Sirt1 interacts with USP22 in the colon cancer HCT116 cell line."
22542455
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"Therefore, USP22 protein interacts with Sirt1."
22542455
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"The zinc finger-containing N terminus of USP22 binds Sirt1."
22542455
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"Furthermore, we found that Sirt1 N terminus interacted with USP22, and this interaction was enhanced by including the HDAC domain of Sirt1."
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"By using Co-immunoprecipitation, the interaction between USP22 and Sirt1 was validated in cells transfected with KLF3-AS1 overexpression plasmid or not (Fig. 4E)."
36627572
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"However, the HDAC domain together with the C terminus of Sirt1 did not interact with USP22 ( Figure 1 E), suggesting that the region between Sirt1 N terminus and its HDAC domain is important for Sirt1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Besides, the direct interaction of USP22 and Sirt1 was validated by co-immunoprecipitation, and the result was consistent with the precious study (Ma et al. 2020)."
36627572
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"USP22 interacts with SIRT1 and removes its polyubiquitin chains, which stabilizes SIRT1."
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"Our studies suggest that SIRT1 and CCNB1 interact with USP22 through different regions."
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"Co-IP results showed that USP22 interacted with SIRT1, but not GPX4 (Fig.  xref A)."
35761309
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"Together with our findings that Sirt1 interacts with USP22, these results indicate that USP22 functions as a bona fide deubiquitinase specifically for Sirt1 and appears to regulate Sirt1 protein stabi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
22542455
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"The ubiquitin-specific peptidase activity of USP22 is required to deubiquitinate Sirt1, as the catalytically inactive USP22 (USP22/C185A) mutant failed to inhibit Sirt1 ubiquitination ( Figures 2 D an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
22542455
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"Therefore, USP22 interacts with Sirt1 via its N terminus to suppress Sirt1 ubiquitination."
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"Consistently, MS and Co‐IP analysis verified the interaction between USP22 and SIRT1 (Figure 5C,D)."
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"43 We took a further step to elucidate the role of USP22/SIRT1 interaction in melanoma metastasis."
39135915
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"In our previous study, USP22 bound to SIRT1 and subsequently activated the AKT pathway, increasing the expression of MRP1 to induce 5-FU resistance in HCC cells [ xref ]."
31587155
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"USP22 directly interacts with SIRT1 based on the co‐immunoprecipitation assay (Fig.  xref B)."
28417539
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"USP22 directly interacts with SIRT1 and then activates AKT/GSK-3β/MRP1, which, in turn, promotes chemotherapeutic efflux in HCC cells ( xref )."
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