{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Panda S"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["457-69"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5677525"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(3)"],"pubmed_abstract":["Whereas phosphorylation of serine, threonine, and tyrosine is exceedingly well characterized, the role of histidine phosphorylation in mammalian signaling is largely unexplored. Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as a phosphohistidine phosphatase that specifically associates with and dephosphorylates the catalytic histidine on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, PGAM5 negatively regulates CD4(+) T cells by inhibiting NDPK-B-mediated histidine phosphorylation and activation of the K(+) channel KCa3.1, which is required for TCR-stimulated Ca(2+) influx and cytokine production. Using recently developed monoclonal antibodies that specifically recognize phosphorylation of nitrogens at the N1 (1-pHis) or N3 (3-pHis) positions o"],"journal":["Molecular cell"],"pubmed_title":["Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4(+) T Cells."],"pmcid":["PMC5677525"],"funding_grant_id":["R01 CA194584","P30 CA016087","T32 CA009370","P30 CA014195","R01 GM099873","R01 CA080100","R01 CA082683"],"pubmed_authors":["Srivastava S","Hunter T","Skolnik EY","Li Z","Panda S","Vaeth M","Fuhs SR"],"additional_accession":[]},"is_claimable":false,"name":"Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4(+) T Cells.","description":"Whereas phosphorylation of serine, threonine, and tyrosine is exceedingly well characterized, the role of histidine phosphorylation in mammalian signaling is largely unexplored. Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as a phosphohistidine phosphatase that specifically associates with and dephosphorylates the catalytic histidine on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, PGAM5 negatively regulates CD4(+) T cells by inhibiting NDPK-B-mediated histidine phosphorylation and activation of the K(+) channel KCa3.1, which is required for TCR-stimulated Ca(2+) influx and cytokine production. Using recently developed monoclonal antibodies that specifically recognize phosphorylation of nitrogens at the N1 (1-pHis) or N3 (3-pHis) positions o","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Aug","modification":"2025-04-19T17:39:46.765Z","creation":"2019-03-27T03:01:14Z"},"accession":"S-EPMC5677525","cross_references":{"pubmed":["27453048"],"doi":["10.1016/j.molcel.2016.06.021"]}}