{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Seervai RNH"],"funding":["National Institute of Environmental Health Sciences","American Heart Association","William and Ella Owens Medical Research Foundation","NIEHS NIH HHS","U.S. Department of Defense","National Cancer Institute","NCI NIH HHS","John Templeton Foundation"],"pagination":["202-208"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8021614"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["558"],"pubmed_abstract":["The process of autophagy is dysregulated in many cancers including clear cell renal cell carcinoma (ccRCC). Autophagy involves the coordination of numerous autophagy-related (ATG) genes, as well as processes involving the actin cytoskeleton. The histone methyltransferase SETD2, frequently inactivated in ccRCC, has recently been shown to also methylate cytoskeletal proteins, which in the case of actin lysine 68 trimethylation (ActK68me3) regulates actin polymerization dynamics. Here we show that cells lacking SETD2 exhibit autophagy defects, as well as decreased interaction of the actin nucleation promoting factor WHAMM with its target actin, which is required for initiation of autophagy. Interestingly, the WHAMM actin binding deficit could be rescued with pharmacologic induction of actin p"],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["An actin-WHAMM interaction linking SETD2 and autophagy."],"pmcid":["PMC8021614"],"funding_grant_id":["R01 CA203012","P30 ES030285","R35 CA231993","P30 CA125123"],"pubmed_authors":["Grimm SL","Coarfa C","Seervai RNH","Tripathi DN","Walker CL","Jangid RK"],"additional_accession":[]},"is_claimable":false,"name":"An actin-WHAMM interaction linking SETD2 and autophagy.","description":"The process of autophagy is dysregulated in many cancers including clear cell renal cell carcinoma (ccRCC). Autophagy involves the coordination of numerous autophagy-related (ATG) genes, as well as processes involving the actin cytoskeleton. The histone methyltransferase SETD2, frequently inactivated in ccRCC, has recently been shown to also methylate cytoskeletal proteins, which in the case of actin lysine 68 trimethylation (ActK68me3) regulates actin polymerization dynamics. Here we show that cells lacking SETD2 exhibit autophagy defects, as well as decreased interaction of the actin nucleation promoting factor WHAMM with its target actin, which is required for initiation of autophagy. Interestingly, the WHAMM actin binding deficit could be rescued with pharmacologic induction of actin p","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2026-04-07T22:16:40.384Z","creation":"2024-11-08T17:58:15.107Z"},"accession":"S-EPMC8021614","cross_references":{"pubmed":["33036756"],"doi":["10.1016/j.bbrc.2020.09.025"]}}