Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1993-05

AUTHORS

N Li, A Batzer, R Daly, V Yajnik, E Skolnik, P Chardin, D Bar-Sagi, B Margolis, J Schlessinger

ABSTRACT

Many of the actions of receptor tyrosine kinases are mediated by the protein Ras, including the activation of various downstream serine/threonine kinases and the stimulation of growth and differentiation. The human protein Grb2 binds to ligand-activated growth factor receptors and downstream effector proteins through its Src-homology (SH) domains SH2 and SH3, respectively, and like its homologue from Caenorhabditis elegans, Sem-5, apparently forms part of a highly conserved pathway by which these receptors can control Ras activity. Here we show that the SH3 domains of Grb2 bind to the carboxy-terminal part of hSos1, the human homologue of the Drosophila guanine-nucleotide-releasing factor for Ras, which is essential for control of Ras activity by epidermal growth factor receptor and sevenless. Moreover, a synthetic 10-amino-acid peptide containing the sequence PPVPPR specifically blocks the interaction. These results indicate that the Grb2/hSos1 complex couples activated EGF receptor to Ras signalling. More... »

PAGES

85-88

Journal

TITLE

Nature

ISSUE

6424

VOLUME

363

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/363085a0

DOI

http://dx.doi.org/10.1038/363085a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011022170

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8479541


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