Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1990-01

AUTHORS

C Ellis, M Moran, F McCormick, T Pawson

ABSTRACT

The critical pathways through which protein-tyrosine kinases induce cellular proliferation and malignant transformation are not well defined. As microinjection of antibodies against p21ras can block the biological effects of both normal and oncogenic tyrosine kinases, it is likely that they require functional p21ras to transmit their mitogenic signals. No biochemical link has been established, however, between tyrosine kinases and p21ras. We have identified a non-catalytic domain of cytoplasmic tyrosine kinases, SH2, that regulates the activity and specificity of the kinase domain. The presence of two adjacent SH2 domains in the p21ras GTPase-activating protein (GAP) indicates that GAP might interact directly with tyrosine kinases. Here we show that GAP, and two co-precipitating proteins of relative molecular masses 62,000 and 190,000 (p62 and p190) are phosphorylated on tyrosine in cells that have been transformed by cytoplasmic and receptor-like tyrosine kinases. The phosphorylation of these polypeptides correlates with transformation in cells expressing inducible forms of the v-src or v-fps encoded tyrosine kinases. Furthermore, GAP, p62 and p190 are also rapidly phosphorylated on tyrosine in fibroblasts stimulated with epidermal growth factor. Our results suggest a mechanism by which tyrosine kinases might modify p21ras function, and implicate GAP and its associated proteins as targets of both oncoproteins and normal growth factor receptors with tyrosine kinase activity. These data support the idea that SH2 sequences direct the interactions of cytoplasmic proteins involved in signal transduction. More... »

PAGES

377

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/343377a0

DOI

http://dx.doi.org/10.1038/343377a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005692180

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1689011


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