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Publication Detail
Binding of G protein beta gamma-subunits to pleckstrin homology domains.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Touhara K, Inglese J, Pitcher JA, Shaw G, Lefkowitz RJ
  • Publication date:
  • Pagination:
    10217, 10220
  • Journal:
    J Biol Chem
  • Volume:
  • Issue:
  • Status:
  • Country:
    United States
  • Print ISSN:
  • Language:
  • Keywords:
    Amino Acid Sequence, Animals, Blood Proteins, Cattle, Cyclic AMP-Dependent Protein Kinases, GTP-Binding Proteins, Glutathione Transferase, Humans, Molecular Sequence Data, Phosphoproteins, Rats, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, beta-Adrenergic Receptor Kinases
Ligand-induced activation of many receptors leads to dissociation of the alpha- and beta gamma-subunit complexes of heterotrimeric G proteins, both of which regulate a variety of effector molecules involved in cellular signaling processes. In one case, a cytosolic enzyme, the beta-adrenergic receptor kinase (beta ARK) binds to the dissociated, prenylated, membrane-anchored beta gamma-subunits of heterotrimeric G proteins (G beta gamma) and is thereby targeted to its membrane-bound receptor substrate. Quite recently, numerous proteins involved in cellular signal transduction have been shown to contain sequences homologous with a "domain" originally identified in the protein "pleckstrin" (pleckstrin homology domain; PH domain) and subsequently found in the G beta gamma interaction region of the beta ARK sequence. Here we demonstrate that glutathione S-transferase-fusion proteins, containing sequences encompassing the PH domain of nine proteins from this group, bind G beta gamma to varying extents. Binding of G beta gamma to these fusion proteins was documented either by a direct binding assay or by ability to block G beta gamma-mediated membrane translocation of beta ARK1. G beta gamma binding to these fusion proteins was inhibited by the alpha subunit of Go (Go alpha), indicating that the binding of G beta gamma to G alpha and the PH domain-containing fusion proteins is mutually exclusive. Studies with a series of truncated PH domains derived from the Ras-guanine-nucleotide-releasing factor indicate that the G beta gamma binding domain includes only the C-terminal portion of the PH domain and sequences just distal to this. Protein-protein interactions between G beta gamma and PH domain-containing proteins may play a significant role in cellular signaling analogous to that previously demonstrated for Src homology 2 and 3 domains.
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