{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kabir M"],"funding":["NCATS NIH HHS","National Cancer Institute","NCI NIH HHS","National Institutes of Health","National Institute of General Medical Sciences","Icahn School of Medicine at Mount Sinai","NIH HHS","NIGMS NIH HHS"],"pagination":["14932-14944"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10357929"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["145(27)"],"pubmed_abstract":["With advances in chemically induced proximity technologies, heterobifunctional modalities such as proteolysis targeting chimeras (PROTACs) have been successfully advanced to clinics for treating cancer. However, pharmacologic activation of tumor-suppressor proteins for cancer treatment remains a major challenge. Here, we present a novel <u>Ace</u>tylation <u>Ta</u>rgeting <u>C</u>himera (AceTAC) strategy to acetylate the p53 tumor suppressor protein. We discovered and characterized the first p53Y220C AceTAC, MS78, which recruits histone acetyltransferase p300/CBP to acetylate the p53Y220C mutant. MS78 effectively acetylated p53Y220C lysine 382 (K382) in a concentration-, time-, and p300-dependent manner and suppressed proliferation and clonogenicity of cancer cells harboring the p53Y220C m"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Acetylation Targeting Chimera Enables Acetylation of the Tumor Suppressor p53."],"pmcid":["PMC10357929"],"funding_grant_id":["R35 CA220491","T32 GM062754","1S10OD025132","T32GM062754","UL1 TR004419","S10 OD025132","1S10OD028504","T32 CA078207","T32CA078207","S10 OD028504"],"pubmed_authors":["Yi J","Xiong Y","Sun N","Kaniskan HU","Hu X","Gu W","Zhong Y","Parsons R","Kabir M","Jin J","Martin TC"],"additional_accession":[]},"is_claimable":false,"name":"Acetylation Targeting Chimera Enables Acetylation of the Tumor Suppressor p53.","description":"With advances in chemically induced proximity technologies, heterobifunctional modalities such as proteolysis targeting chimeras (PROTACs) have been successfully advanced to clinics for treating cancer. However, pharmacologic activation of tumor-suppressor proteins for cancer treatment remains a major challenge. Here, we present a novel <u>Ace</u>tylation <u>Ta</u>rgeting <u>C</u>himera (AceTAC) strategy to acetylate the p53 tumor suppressor protein. We discovered and characterized the first p53Y220C AceTAC, MS78, which recruits histone acetyltransferase p300/CBP to acetylate the p53Y220C mutant. MS78 effectively acetylated p53Y220C lysine 382 (K382) in a concentration-, time-, and p300-dependent manner and suppressed proliferation and clonogenicity of cancer cells harboring the p53Y220C m","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jul","modification":"2025-04-05T15:48:13.414Z","creation":"2025-04-05T15:48:13.414Z"},"accession":"S-EPMC10357929","cross_references":{"pubmed":["37365684"],"doi":["10.1021/jacs.3c04640"]}}