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Molecular cloning of a novel phosphorylation‐dependent inhibitory protein of protein phosphatase‐1 (CPI17) in smooth muscle: its specific localization in smooth muscle 1
Author(s) -
Eto Masumi,
Senba Shingo,
Morita Fumi,
Yazawa Michio
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00657-1
Subject(s) - phosphorylation , protein phosphatase 1 , phosphatase , complementary dna , microbiology and biotechnology , inhibitory postsynaptic potential , biology , biochemistry , messenger rna , cdna library , recombinant dna , peptide sequence , skeletal muscle , chemistry , endocrinology , gene
The cDNA encoding a phosphorylation‐dependent inhibitory protein of protein phosphatase‐1 (PP1) was isolated from a porcine aorta library. The coding region represented the complete amino acid sequence of this protein comprised of a novel 147‐residue polypeptide, which we termed CPI17, a 17‐kDa PKC‐potentiated inhibitory protein of PP1. As well as the native CPI17 from porcine aorta, the recombinant protein completely suppressed the PP1 activity (IC 50 =0.18 nM) by the stoichiometric thiophosphorylation. The CPI17 mRNA is expressed in smooth muscle tissues such as aorta and bladder, whereas little expression was observed in heart, skeletal muscle, and non‐muscle tissues. These results suggest a specific regulatory mechanism of the PP1 activity through CPI17 in smooth muscle.