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Publication Detail
The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Pitcher JA, Payne ES, Csortos C, DePaoli-Roach AA, Lefkowitz RJ
  • Publication date:
    29/08/1995
  • Pagination:
    8343, 8347
  • Journal:
    Proc Natl Acad Sci U S A
  • Volume:
    92
  • Issue:
    18
  • Country:
    UNITED STATES
  • Print ISSN:
    0027-8424
  • Language:
    eng
  • Keywords:
    Animals, Blotting, Western, Brain, Cattle, Cell Membrane, Chromatography, Gel, GTP-Binding Proteins, Humans, Phosphoprotein Phosphatases, Receptor Protein-Tyrosine Kinases, Receptors, Cell Surface, Spodoptera, Subcellular Fractions, Substrate Specificity
Abstract
Phosphorylation of G-protein-coupled receptors plays an important role in regulating their function. In this study the G-protein-coupled receptor phosphatase (GRP) capable of dephosphorylating G-protein-coupled receptor kinase-phosphorylated receptors is described. The GRP activity of bovine brain is a latent oligomeric form of protein phosphatase type 2A (PP-2A) exclusively associated with the particulate fraction. GRP activity is observed only when assayed in the presence of protamine or when phosphatase-containing fractions are subjected to freeze/thaw treatment under reducing conditions. Consistent with its identification as a member of the PP-2A family, the GRP is potently inhibited by okadaic acid but not by I-2, the specific inhibitor of protein phosphatase type 1. Solubilization of the membrane-associated GRP followed by gel filtration in the absence of detergent yields a 150-kDa peak of latent receptor phosphatase activity. Western blot analysis of this phosphatase reveals a likely subunit composition of AB alpha C. PP-2A of this subunit composition has previously been characterized as a soluble enzyme, yet negligible soluble GRP activity was observed. The subcellular distribution and substrate specificity of the GRP suggests significant differences between it and previously characterized forms of PP-2A.
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