{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wilkins JM"],"funding":["NCCIH NIH HHS","National Institutes of Health"],"pagination":["25137-48"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4155678"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(36)"],"pubmed_abstract":["Phosphoglycerate mutase 5 (PGAM5) is an atypical mitochondrial Ser/Thr phosphatase that modulates mitochondrial dynamics and participates in both apoptotic and necrotic cell death. The mechanisms that regulate the phosphatase activity of PGAM5 are poorly understood. The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology with the catalytic domains found in other members of the phosphoglycerate mutase family, including a conserved histidine that is absolutely required for catalytic activity. However, this conserved domain is not sufficient for maximal phosphatase activity. We have identified a highly conserved amino acid motif, WDXNWD, located within the unique N-terminal region, which is required for assembly of PGAM5 into large multimeric complexes. Alanine substitutions wi"],"journal":["The Journal of biological chemistry"],"pubmed_title":["A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5."],"pmcid":["PMC4155678"],"funding_grant_id":["P50AT006273","P50 AT006273"],"pubmed_authors":["Tipton PA","Hannink M","Wilkins JM","McConnell C"],"additional_accession":[]},"is_claimable":false,"name":"A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5.","description":"Phosphoglycerate mutase 5 (PGAM5) is an atypical mitochondrial Ser/Thr phosphatase that modulates mitochondrial dynamics and participates in both apoptotic and necrotic cell death. The mechanisms that regulate the phosphatase activity of PGAM5 are poorly understood. The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology with the catalytic domains found in other members of the phosphoglycerate mutase family, including a conserved histidine that is absolutely required for catalytic activity. However, this conserved domain is not sufficient for maximal phosphatase activity. We have identified a highly conserved amino acid motif, WDXNWD, located within the unique N-terminal region, which is required for assembly of PGAM5 into large multimeric complexes. Alanine substitutions wi","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Sep","modification":"2025-04-04T12:08:52.126Z","creation":"2019-03-27T01:35:15Z"},"accession":"S-EPMC4155678","cross_references":{"pubmed":["25012655"],"doi":["10.1074/jbc.M114.565549","10.1074/jbc.m114.565549"]}}