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• W2023859626 endingPage "14061" @default.
• W2023859626 startingPage "14053" @default.
• W2023859626 abstract "NIPP-1 is a subunit of the major nuclear protein phosphatase-1 (PP-1) in mammalian cells and potently inhibits PP-1 activity in vitro. Using yeast two-hybrid and co-sedimentation assays, we mapped a PP-1-binding site and the inhibition function to the central one-third domain of NIPP-1. Full-length NIPP-1 (351 residues) and the central domain, NIPP-1143–217, were equally potent PP-1 inhibitors (IC50 = 0.3 nm). Synthetic peptides spanning the central domain of NIPP-1 further narrowed the PP-1 inhibitory function to residues 191–200. A second, noninhibitory PP-1-binding site was identified by far-Western assays with digoxygenin-conjugated catalytic subunit (PP-1C) and included a consensus RVXF motif (residues 200–203) found in many other PP-1-binding proteins. The substitutions, V201A and/or F203A, in the RVXF motif, or phosphorylation of Ser199 or Ser204, which are established phosphorylation sites for protein kinase A and protein kinase CK2, respectively, prevented PP-1C-binding by NIPP-1191–210 in the far-Western assay. NIPP-1191–210 competed for PP-1 inhibition by full-length NIPP-11–351, inhibitor-1 and inhibitor-2, and dissociated PP-1C from inhibitor-1- and NIPP-1143–217-Sepharose but not from full-length NIPP-11–351-Sepharose. Together, these data identified some of the key elements in the central domain of NIPP-1 that regulate PP-1 activity and suggested that the flanking sequences stabilize the association of NIPP-1 with PP-1C." @default.
• W2023859626 created "2016-06-24" @default.
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• W2023859626 date "1999-05-01" @default.
• W2023859626 modified "2023-09-27" @default.
• W2023859626 title "Molecular Determinants of Nuclear Protein Phosphatase-1 Regulation by NIPP-1" @default.
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• W2023859626 doi "https://doi.org/10.1074/jbc.274.20.14053" @default.
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