{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Olea-Flores M"],"funding":["National Institute of Arthritis and Musculoskeletal and Skin Diseases","NIAMS NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e23702"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11268309"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["38(11)"],"pubmed_abstract":["Pyruvate kinase is a glycolytic enzyme that converts phosphoenolpyruvate and ADP into pyruvate and ATP. There are two genes that encode pyruvate kinase in vertebrates; Pkm and Pkl encode muscle- and liver/erythrocyte-specific forms, respectively. Each gene encodes two isoenzymes due to alternative splicing. Both muscle-specific enzymes, PKM1 and PKM2, function in glycolysis, but PKM2 also has been implicated in gene regulation due to its ability to phosphorylate histone 3 threonine 11 (H3T11) in cancer cells. Here, we examined the roles of PKM1 and PKM2 during myoblast differentiation. RNA-seq analysis revealed that PKM2 promotes the expression of Dpf2/Baf45d and Baf250a/Arid1A. DPF2 and BAF250a are subunits that identify a specific sub-family of the mammalian SWI/SNF (mSWI/SNF) of chromat"],"journal":["FASEB journal : official publication of the Federation of American Societies for Experimental Biology"],"pubmed_title":["Muscle-specific pyruvate kinase isoforms, PKM1 and PKM2, regulate mammalian SWI/SNF proteins and histone 3 phosphorylation during myoblast differentiation."],"pmcid":["PMC11268309"],"funding_grant_id":["R35 GM118112","R35 GM136393","R35 GM136392","R01 AR077578"],"pubmed_authors":["Padilla-Benavides T","Olea-Flores M","Sharma T","DiBartolomeo I","Verdejo-Torres O","Thompson PR","Imbalzano AN"],"additional_accession":[]},"is_claimable":false,"name":"Muscle-specific pyruvate kinase isoforms, PKM1 and PKM2, regulate mammalian SWI/SNF proteins and histone 3 phosphorylation during myoblast differentiation.","description":"Pyruvate kinase is a glycolytic enzyme that converts phosphoenolpyruvate and ADP into pyruvate and ATP. There are two genes that encode pyruvate kinase in vertebrates; Pkm and Pkl encode muscle- and liver/erythrocyte-specific forms, respectively. Each gene encodes two isoenzymes due to alternative splicing. Both muscle-specific enzymes, PKM1 and PKM2, function in glycolysis, but PKM2 also has been implicated in gene regulation due to its ability to phosphorylate histone 3 threonine 11 (H3T11) in cancer cells. Here, we examined the roles of PKM1 and PKM2 during myoblast differentiation. RNA-seq analysis revealed that PKM2 promotes the expression of Dpf2/Baf45d and Baf250a/Arid1A. DPF2 and BAF250a are subunits that identify a specific sub-family of the mammalian SWI/SNF (mSWI/SNF) of chromat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-07-15T01:49:12.932Z","creation":"2026-06-27T03:17:55.581Z"},"accession":"S-EPMC11268309","cross_references":{"pubmed":["38837439"],"doi":["10.1096/fj.202400784R","10.1096/fj.202400784r"]}}