IndraLab

Statements

USP22 leads to the deacetylation of TP53. 7 / 7
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"The deacetylase activity of Sirt1 is required for its synergy with USP22 in suppressing p53 acetylation, as expression of the HDAC inactive mutant of Sirt1, Sirt1/HY, failed to inhibit p53 acetylation[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Notably, expression of USP22 failed to suppress p53 acetylation in sirt1 knockdown HCT116 cells ( Figure S3 A) or in sirt1 null MEF cells ( Figure 5 C)."
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"Therefore, our studies collectively demonstrated that USP22-mediated deubiquitination of Sirt1 inhibits p53 acetylation and transcriptional activity and p53-mediated apoptosis in response to DNA damag[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP22 overexpression can increase the SIRT1 protein level and decrease the p53 acetylation level, promoting SLC7A11 expression."
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"Ubiquitin-specific peptidase 22 stabilizes sirtuin 1 (SIRT1) through deubiquitination, and increased SIRT1 expression results in decreased p53 acetylation and protein expression."
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"USP22 mediated stabilization of Sirt1 results in decreased levels of p53 acetylation and consequently in suppression of p53 mediated functions."
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"As shown in Figure 5 A , USP22 and Sirt1 synergistically inhibited p53 acetylation."
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