<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Olea-Flores M</submitter><funding>National Institute of Arthritis and Musculoskeletal and Skin Diseases</funding><funding>NIAMS NIH HHS</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>e23702</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11268309</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>38(11)</volume><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</pubmed_abstract><journal>FASEB journal : official publication of the Federation of American Societies for Experimental Biology</journal><pubmed_title>Muscle-specific pyruvate kinase isoforms, PKM1 and PKM2, regulate mammalian SWI/SNF proteins and histone 3 phosphorylation during myoblast differentiation.</pubmed_title><pmcid>PMC11268309</pmcid><funding_grant_id>R35 GM118112</funding_grant_id><funding_grant_id>R35 GM136393</funding_grant_id><funding_grant_id>R35 GM136392</funding_grant_id><funding_grant_id>R01 AR077578</funding_grant_id><pubmed_authors>Padilla-Benavides T</pubmed_authors><pubmed_authors>Olea-Flores M</pubmed_authors><pubmed_authors>Sharma T</pubmed_authors><pubmed_authors>DiBartolomeo I</pubmed_authors><pubmed_authors>Verdejo-Torres O</pubmed_authors><pubmed_authors>Thompson PR</pubmed_authors><pubmed_authors>Imbalzano AN</pubmed_authors></additional><is_claimable>false</is_claimable><name>Muscle-specific pyruvate kinase isoforms, PKM1 and PKM2, regulate mammalian SWI/SNF proteins and histone 3 phosphorylation during myoblast differentiation.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jun</publication><modification>2026-07-15T01:49:12.932Z</modification><creation>2026-06-27T03:17:55.581Z</creation></dates><accession>S-EPMC11268309</accession><cross_references><pubmed>38837439</pubmed><doi>10.1096/fj.202400784R</doi><doi>10.1096/fj.202400784r</doi></cross_references></HashMap>