biostudies-literatureChoy MSHHS | NIH | National Institute of General Medical SciencesHHS | NIH | National Institute of Neurological Disorders and Stroke (NINDS)HHS | NIH | National Institute of Neurological Disorders and StrokeNINDS NIH HHSNCI NIH HHSHHS | NIH | National Institute of General Medical Sciences (NIGMS)NIGMS NIH HHSe2415383121https://www.ebi.ac.uk/biostudies/studies/S-EPMC11536154biostudies-literatureUnknown121(44)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 arProceedings of the National Academy of Sciences of the United States of AmericaA protein phosphatase 1 specific <i>phos</i>phatase <i>ta</i>rgeting <i>p</i>eptide (PhosTAP) to identify the PP1 phosphatome.PMC11536154P30 CA023108P41 GM103393R01 NS091336R01GM144379R01 NS124666R01 GM144483R35 GM119455R01NS124666R01 GM144379R35GM119455R01 GM134683R01GM134683Kumar GSPeti WKettenbach ANChoy MSPage RNguyen HTfalseA protein phosphatase 1 specific <i>phos</i>phatase <i>ta</i>rgeting <i>p</i>eptide (PhosTAP) to identify the PP1 phosphatome.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 ar2024-01-01T00:00:00Z2024 Oct2026-06-03T00:22:40.477Z2025-04-04T23:31:47.603ZS-EPMC115361543944638910.1073/pnas.2415383121