{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Choy MS"],"funding":["HHS | NIH | National Institute of General Medical Sciences","HHS | NIH | National Institute of Neurological Disorders and Stroke (NINDS)","HHS | NIH | National Institute of Neurological Disorders and Stroke","NINDS NIH HHS","NCI NIH HHS","HHS | NIH | National Institute of General Medical Sciences (NIGMS)","NIGMS NIH HHS"],"pagination":["e2415383121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11536154"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(44)"],"pubmed_abstract":["Phosphoprotein phosphatases (PPPs) are the key serine/threonine phosphatases that regulate all essential signaling cascades. In particular, Protein Phosphatase 1 (PP1) dephosphorylates ~80% of all ser/thr phosphorylation sites. Here, we developed a phosphatase targeting peptide (PhosTAP) that binds all PP1 isoforms and does so with a stronger affinity than any other known PP1 regulator. This PhosTAP can be used as a PP1 recruitment tool for Phosphorylation Targeting Chimera (PhosTAC)-type recruitment in in vitro and cellular experiments, as well as in phosphoproteomics experiments to identify PP1-specific substrates and phosphosites. The latter is especially important to further our understanding of cellular signaling, as the identification of substrates and especially phosphosites that ar"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["A protein phosphatase 1 specific <i>phos</i>phatase <i>ta</i>rgeting <i>p</i>eptide (PhosTAP) to identify the PP1 phosphatome."],"pmcid":["PMC11536154"],"funding_grant_id":["P30 CA023108","P41 GM103393","R01 NS091336","R01GM144379","R01 NS124666","R01 GM144483","R35 GM119455","R01NS124666","R01 GM144379","R35GM119455","R01 GM134683","R01GM134683"],"pubmed_authors":["Kumar GS","Peti W","Kettenbach AN","Choy MS","Page R","Nguyen HT"],"additional_accession":[]},"is_claimable":false,"name":"A protein phosphatase 1 specific <i>phos</i>phatase <i>ta</i>rgeting <i>p</i>eptide (PhosTAP) to identify the PP1 phosphatome.","description":"Phosphoprotein phosphatases (PPPs) are the key serine/threonine phosphatases that regulate all essential signaling cascades. In particular, Protein Phosphatase 1 (PP1) dephosphorylates ~80% of all ser/thr phosphorylation sites. Here, we developed a phosphatase targeting peptide (PhosTAP) that binds all PP1 isoforms and does so with a stronger affinity than any other known PP1 regulator. This PhosTAP can be used as a PP1 recruitment tool for Phosphorylation Targeting Chimera (PhosTAC)-type recruitment in in vitro and cellular experiments, as well as in phosphoproteomics experiments to identify PP1-specific substrates and phosphosites. The latter is especially important to further our understanding of cellular signaling, as the identification of substrates and especially phosphosites that ar","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-06-03T00:22:40.477Z","creation":"2025-04-04T23:31:47.603Z"},"accession":"S-EPMC11536154","cross_references":{"pubmed":["39446389"],"doi":["10.1073/pnas.2415383121"]}}