Tyrosine phosphorylation of G protein alpha subunits by pp60c-src.
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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Related Subject Headings
- Tyrosine
- Structure-Activity Relationship
- Signal Transduction
- Proto-Oncogene Proteins pp60(c-src)
- Protein Conformation
- Phosphotyrosine
- Phosphorylation
- Phosphoproteins
- Guanosine 5'-O-(3-Thiotriphosphate)
- Guanine Nucleotides
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Tyrosine
- Structure-Activity Relationship
- Signal Transduction
- Proto-Oncogene Proteins pp60(c-src)
- Protein Conformation
- Phosphotyrosine
- Phosphorylation
- Phosphoproteins
- Guanosine 5'-O-(3-Thiotriphosphate)
- Guanine Nucleotides