{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gong L"],"funding":["American Heart Association","U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","National Natural Science Foundation of China","NIGMS NIH HHS"],"pagination":["6781"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9645763"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Polycomb repressive complex 2 (PRC2) plays a key role in maintaining cell identity during differentiation. Methyltransferase activity of PRC2 on histone H3 lysine 27 is regulated by diverse cellular mechanisms, including posttranslational modification. Here, we report a unique phosphorylation-dependent mechanism stimulating PRC2 enzymatic activity. Residue S583 of SUZ12 is phosphorylated by casein kinase 2 (CK2) in cells. A crystal structure captures phosphorylation in action: the flexible phosphorylation-dependent stimulation loop harboring S583 becomes engaged with the catalytic SET domain through a phosphoserine-centered interaction network, stabilizing the enzyme active site and in particular S-adenosyl-methionine (SAM)-binding pocket. CK2-mediated S583 phosphorylation promotes catalys"],"journal":["Nature communications"],"pubmed_title":["CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site."],"pmcid":["PMC9645763"],"funding_grant_id":["GM121662","19POST34450043","32071213","P41 GM103393","GM136308","R35 GM136308","R01 GM121662"],"pubmed_authors":["Liu X","Yang X","Jiao L","Lemoff A","Gong L"],"additional_accession":[]},"is_claimable":false,"name":"CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site.","description":"Polycomb repressive complex 2 (PRC2) plays a key role in maintaining cell identity during differentiation. Methyltransferase activity of PRC2 on histone H3 lysine 27 is regulated by diverse cellular mechanisms, including posttranslational modification. Here, we report a unique phosphorylation-dependent mechanism stimulating PRC2 enzymatic activity. Residue S583 of SUZ12 is phosphorylated by casein kinase 2 (CK2) in cells. A crystal structure captures phosphorylation in action: the flexible phosphorylation-dependent stimulation loop harboring S583 becomes engaged with the catalytic SET domain through a phosphoserine-centered interaction network, stabilizing the enzyme active site and in particular S-adenosyl-methionine (SAM)-binding pocket. CK2-mediated S583 phosphorylation promotes catalys","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-07-14T15:08:37.687Z","creation":"2025-04-19T22:47:12.631Z"},"accession":"S-EPMC9645763","cross_references":{"pubmed":["36351927"],"doi":["10.1038/s41467-022-34431-1"]}}