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Publication Detail
Tyrosine phosphorylation of G protein alpha subunits by pp60c-src.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Hausdorff WP, Pitcher JA, Luttrell DK, Linder ME, Kurose H, Parsons SJ, Caron MG, Lefkowitz RJ
  • Publication date:
    01/07/1992
  • Pagination:
    5720, 5724
  • Journal:
    Proc Natl Acad Sci U S A
  • Volume:
    89
  • Issue:
    13
  • Country:
    UNITED STATES
  • Print ISSN:
    0027-8424
  • Language:
    eng
  • Keywords:
    Animals, Fluorides, GTP-Binding Proteins, Guanine Nucleotides, Guanosine 5'-O-(3-Thiotriphosphate), Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein Conformation, Proto-Oncogene Proteins pp60(c-src), Signal Transduction, Structure-Activity Relationship, Tyrosine
Abstract
A number of lines of evidence suggest that cross-talk exists between the cellular signal transduction pathways involving tyrosine phosphorylation catalyzed by members of the pp60c-src kinase family and those mediated by guanine nucleotide regulatory proteins (G proteins). In this study, we explore the possibility that direct interactions between pp60c-src and G proteins may occur with functional consequences. Preparations of pp60c-src isolated by immunoprecipitation phosphorylate on tyrosine residues the purified G-protein alpha subunits (G alpha) of several heterotrimeric G proteins. Phosphorylation is highly dependent on G-protein conformation, and G alpha(GDP) uncomplexed by beta gamma subunits appears to be the preferred substrate. In functional studies, phosphorylation of stimulatory G alpha (G alpha s) modestly increases the rate of binding of guanosine 5'-[gamma-[35S]thio]triphosphate to Gs as well as the receptor-stimulated steady-state rate of GTP hydrolysis by Gs. Heterotrimeric G proteins may represent a previously unappreciated class of potential substrates for pp60c-src.
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