Tyrosine phosphorylation of G protein α subunits by pp60c-src

William P. Hausdorff, Julie A. Pitcher, Deirdre K. Luttrell, Maurine E. Linder, Hitoshi Kurose, Sarah J. Parsons, Marc G. Caron, Robert J. Lefkowitz

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102 Citations (Scopus)

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 a subunits (Gα) of several heterotrimeric G proteins. Phosphorylation is highly dependent on G-protein conformation, and Gα(GDP) uncomplexed by βγ subunits appears to be the preferred substrate. In functional studies, phosphorylation of stimulatory Gα (Gαs) modestly increases the rate of binding of guanosine 5′-[γ-[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.

Original languageEnglish
Pages (from-to)5720-5724
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number13
Publication statusPublished - Jul 1 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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