{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pena IA"],"funding":["NIDA NIH HHS","NHLBI NIH HHS","NCI NIH HHS","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["978"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11760969"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Many essential proteins require pyridoxal 5'-phosphate, the active form of vitamin B6, as a cofactor for their activity. These include enzymes important for amino acid metabolism, one-carbon metabolism, polyamine synthesis, erythropoiesis, and neurotransmitter metabolism. A third of all mammalian pyridoxal 5'-phosphate-dependent enzymes are localized in the mitochondria; however, the molecular machinery involved in the regulation of mitochondrial pyridoxal 5'-phosphate levels in mammals remains unknown. In this study, we used a genome-wide CRISPR interference screen in erythroleukemia cells and organellar metabolomics to identify the mitochondrial inner membrane protein SLC25A38 as a regulator of mitochondrial pyridoxal 5'-phosphate. Loss of SLC25A38 causes depletion of mitochondrial, but "],"journal":["Nature communications"],"pubmed_title":["SLC25A38 is required for mitochondrial pyridoxal 5'-phosphate (PLP) accumulation."],"pmcid":["PMC11760969"],"funding_grant_id":["F31 CA228241","F30 CA268633","T32 GM007287","T32 GM144273","T32 HL007118","P30 CA014051","R35 GM151097","T32 GM007753","F31 NS127458","R00 CA241332","P30 DA018343","R35 CA242379"],"pubmed_authors":["Yang J","Vander Heiden MG","Sienski G","Adelmann CH","Nairn AC","Lewis CA","Ge P","Sabatini DM","Block S","Bathla S","Kory N","Pena IA","Shi JS","Keys HR","Witham IH","Chang SM","Heiman M"],"additional_accession":[]},"is_claimable":false,"name":"SLC25A38 is required for mitochondrial pyridoxal 5'-phosphate (PLP) accumulation.","description":"Many essential proteins require pyridoxal 5'-phosphate, the active form of vitamin B6, as a cofactor for their activity. These include enzymes important for amino acid metabolism, one-carbon metabolism, polyamine synthesis, erythropoiesis, and neurotransmitter metabolism. A third of all mammalian pyridoxal 5'-phosphate-dependent enzymes are localized in the mitochondria; however, the molecular machinery involved in the regulation of mitochondrial pyridoxal 5'-phosphate levels in mammals remains unknown. In this study, we used a genome-wide CRISPR interference screen in erythroleukemia cells and organellar metabolomics to identify the mitochondrial inner membrane protein SLC25A38 as a regulator of mitochondrial pyridoxal 5'-phosphate. Loss of SLC25A38 causes depletion of mitochondrial, but ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-02T07:11:15.056Z","creation":"2025-04-05T00:25:36.274Z"},"accession":"S-EPMC11760969","cross_references":{"pubmed":["39856062"],"doi":["10.1038/s41467-025-56130-3"]}}