The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-05

AUTHORS

Maria Rozakis-Adcock, Ross Fernley, John Wade, Tony Pawson, David Bowtell

ABSTRACT

MANY tyrosine kinases, including the receptors for hormones such as epidermal growth factor (EGF), nerve growth factor and insulin, transmit intracellular signals through Ras proteins1–4. Ligand binding to such receptors stimulates Ras guanine-nucleotide-exchange activity5–9 and increases the level of GTP-bound Ras10–12, suggesting that these tyrosine kinases may activate a guanine-nucleotide releasing protein (GNRP). In Caenorhabditis elegans and Drosophila, genetic studies have shown that Ras activation by tyrosine kinases requires the protein Sem-5/drk, which contains a single Src-homology (SH) 2 domain and two flanking SH3 domains13–15. Sem-5 is homologous to the mammalian protein Grb2, which binds the autophosphorylated EGF receptor and other phosphotyrosine-containing proteins such as Shc through its SH2 domain16,17. Here we show that in rodent fibroblasts, the SH3 domains of Grb2 are bound to the proline-rich carboxy-terminal tail of mSos1, a protein homologous to Drosophila Sos. Sos is required for Ras signalling18–20 and contains a central domain related to known Ras-GNRPs21–23. EGF stimulation induces binding of the Grb2-mSos1 complex to the autophosphorylated EGF receptor, and mSos1 phosphorylation. Grb2 therefore appears to link tyrosine kinases to a Ras-GNRP in mammalian cells. More... »

PAGES

83-85

Journal

TITLE

Nature

ISSUE

6424

VOLUME

363

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/363083a0

DOI

http://dx.doi.org/10.1038/363083a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022031225

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8479540


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