{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["18(7)"],"submitter":["Ouyang C"],"pubmed_abstract":["SIRT1 (silent mating type information regulation 2 homolog 1), a class III histone deacetylase, is known to participate in multiple steps of the DNA damage response (DDR) by deacetylating several key DDR proteins. At present, the mechanisms regulating SIRT1 protein stability upon DNA damage have yet to be fully elucidated. In this study, we reveal that, under severe DNA damage, SIRT1 undergoes two forms of post-translational modifications (PTMs): (i) increased polyubiquitination and proteasomal degradation mediated by TRIM28 (tripartite motif-containing protein 28), a RING-domain E3 ligase; and (ii) cleavage at C-terminal mediated by caspases. Importantly, there is reciprocal effects between these forms of PTMs: while suppression of proteasome reduces caspases-mediated cleavage, the cleave"],"journal":["International journal of biological sciences"],"pagination":["2655-2669"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9066097"],"repository":["biostudies-literature"],"pubmed_title":["Post-translational Modification in Control of SIRT1 Stability during DNA Damage Response."],"pmcid":["PMC9066097"],"pubmed_authors":["Ouyang C","Bay BH","Lu G","He W","Shen HM"],"additional_accession":[]},"is_claimable":false,"name":"Post-translational Modification in Control of SIRT1 Stability during DNA Damage Response.","description":"SIRT1 (silent mating type information regulation 2 homolog 1), a class III histone deacetylase, is known to participate in multiple steps of the DNA damage response (DDR) by deacetylating several key DDR proteins. At present, the mechanisms regulating SIRT1 protein stability upon DNA damage have yet to be fully elucidated. In this study, we reveal that, under severe DNA damage, SIRT1 undergoes two forms of post-translational modifications (PTMs): (i) increased polyubiquitination and proteasomal degradation mediated by TRIM28 (tripartite motif-containing protein 28), a RING-domain E3 ligase; and (ii) cleavage at C-terminal mediated by caspases. Importantly, there is reciprocal effects between these forms of PTMs: while suppression of proteasome reduces caspases-mediated cleavage, the cleave","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-30T15:17:23.557Z","creation":"2025-04-04T10:01:54.31Z"},"accession":"S-EPMC9066097","cross_references":{"pubmed":["35541916"],"doi":["10.7150/ijbs.68587"]}}