{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen CW"],"funding":["U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI)","Ministry of Science and Technology, Taiwan","Ministry of Science and Technology, Taiwan (Ministry of Science and Technology of Taiwan)","U.S. Department of Health & Human Services | NIH | National Cancer Institute","NCI NIH HHS"],"pagination":["2264"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10938004"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["NME3 is a member of the nucleoside diphosphate kinase (NDPK) family localized on the mitochondrial outer membrane (MOM). Here, we report a role of NME3 in hypoxia-induced mitophagy dependent on its active site phosphohistidine but not the NDPK function. Mice carrying a knock-in mutation in the Nme3 gene disrupting NME3 active site histidine phosphorylation are vulnerable to ischemia/reperfusion-induced infarction and develop abnormalities in cerebellar function. Our mechanistic analysis reveals that hypoxia-induced phosphatidic acid (PA) on mitochondria is essential for mitophagy and the interaction of DRP1 with NME3. The PA binding function of MOM-localized NME3 is required for hypoxia-induced mitophagy. Further investigation demonstrates that the interaction with active NME3 prevents DRP"],"journal":["Nature communications"],"pubmed_title":["NME3 is a gatekeeper for DRP1-dependent mitophagy in hypoxia."],"pmcid":["PMC10938004"],"funding_grant_id":["NSCT 111-2326-B-002-022","CA242443","NSCT 111-2634-F-002-017","NSCT 111-2320-B-002-088","R35 CA242443"],"pubmed_authors":["Hunter T","Su C","Feng Y","Hsieh ST","Chang ZF","Cuili X","Fan CH","Ting CW","Yeh TY","Huang CY","Tsai YW","Chen YJ","Yang KC","Huang XR","Chao T","Chen CW"],"additional_accession":[]},"is_claimable":false,"name":"NME3 is a gatekeeper for DRP1-dependent mitophagy in hypoxia.","description":"NME3 is a member of the nucleoside diphosphate kinase (NDPK) family localized on the mitochondrial outer membrane (MOM). Here, we report a role of NME3 in hypoxia-induced mitophagy dependent on its active site phosphohistidine but not the NDPK function. Mice carrying a knock-in mutation in the Nme3 gene disrupting NME3 active site histidine phosphorylation are vulnerable to ischemia/reperfusion-induced infarction and develop abnormalities in cerebellar function. Our mechanistic analysis reveals that hypoxia-induced phosphatidic acid (PA) on mitochondria is essential for mitophagy and the interaction of DRP1 with NME3. The PA binding function of MOM-localized NME3 is required for hypoxia-induced mitophagy. Further investigation demonstrates that the interaction with active NME3 prevents DRP","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-07-15T12:01:47.972Z","creation":"2026-07-04T03:12:28.459Z"},"accession":"S-EPMC10938004","cross_references":{"pubmed":["38480688"],"doi":["10.1038/s41467-024-46385-7"]}}