{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sreedevi K"],"funding":["NHLBI NIH HHS"],"pagination":["1-12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12646366"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["198"],"pubmed_abstract":["PERM1 was initially identified as a new downstream target of PGC-1α and ERRs that regulates mitochondrial bioenergetics in skeletal muscle. Subsequently, we and other groups demonstrated that PERM1 is also a positive regulator of mitochondrial bioenergetics in the heart. However, the exact mechanisms of regulatory functions of PERM1 remain poorly understood. O-GlcNAcylation is a post-translational modification of proteins that are regulated by two enzymes: O-GlcNAc transferase (OGT) that adds O-GlcNAc to proteins; O-GlcNAcase (OGA) that removes O-GlcNAc from proteins. O-GlcNAcylation is a powerful signaling mechanism mediating cellular responses to stressors and nutrient availability, which, among other targets, may influence cardiac metabolism. We hypothesized that PERM1 regulates mitocho"],"journal":["Journal of molecular and cellular cardiology"],"pubmed_title":["PERM1 regulates mitochondrial energetics through O-GlcNAcylation in the heart."],"pmcid":["PMC12646366"],"funding_grant_id":["R01 HL156667"],"pubmed_authors":["Wende AR","Warren JS","Zaitsev AV","James A","Yedla S","Arowa S","Sreedevi K","Do S","Oka SI"],"additional_accession":[]},"is_claimable":false,"name":"PERM1 regulates mitochondrial energetics through O-GlcNAcylation in the heart.","description":"PERM1 was initially identified as a new downstream target of PGC-1α and ERRs that regulates mitochondrial bioenergetics in skeletal muscle. Subsequently, we and other groups demonstrated that PERM1 is also a positive regulator of mitochondrial bioenergetics in the heart. However, the exact mechanisms of regulatory functions of PERM1 remain poorly understood. O-GlcNAcylation is a post-translational modification of proteins that are regulated by two enzymes: O-GlcNAc transferase (OGT) that adds O-GlcNAc to proteins; O-GlcNAcase (OGA) that removes O-GlcNAc from proteins. O-GlcNAcylation is a powerful signaling mechanism mediating cellular responses to stressors and nutrient availability, which, among other targets, may influence cardiac metabolism. We hypothesized that PERM1 regulates mitocho","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-06T08:57:12.519Z","creation":"2026-05-28T03:11:32.092Z"},"accession":"S-EPMC12646366","cross_references":{"pubmed":["39581161"],"doi":["10.1016/j.yjmcc.2024.11.002"]}}