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Science 25 June 1993:
Vol. 260. no. 5116, pp. 1950 - 1952
DOI: 10.1126/science.8391166
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Articles

Science, Vol 260, Issue 5116, 1950-1952
Copyright © 1993 by American Association for the Advancement of Science

articles

Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes

K Baltensperger, LM Kozma, AD Cherniack, JK Klarlund, A Chawla, U Banerjee, and MP Czech

Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.

Signal transmission by insulin involves tyrosine phosphorylation of a major insulin receptor substrate (IRS-1) and exchange of Ras-bound guanosine diphosphate for guanosine triphosphate. Proteins containing Src homology 2 and 3 (SH2 and SH3) domains, such as the p85 regulatory subunit of phosphatidylinositol-3 kinase and growth factor receptor-bound protein 2 (GRB2), bind tyrosine phosphate sites on IRS-1 through their SH2 regions. Such complexes in COS cells were found to contain the heterologously expressed putative guanine nucleotide exchange factor encoded by the Drosophila son of sevenless gene (dSos). Thus, GRB2, p85, or other proteins with SH2-SH3 adapter sequences may link Sos proteins to IRS-1 signaling complexes as part of the mechanism by which insulin activates Ras.


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Shc Isoform-specific Tyrosine Phosphorylation by the Insulin and Epidermal Growth Factor Receptors.
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Interleukin-13 Signal Transduction in Lymphohemopoietic Cells.
M. J. Welham, L. Learmonth, H. Bone, and J. W. Schrader (1995)
J. Biol. Chem. 270, 12286-12296
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J. Biol. Chem. 270, 7712-7716
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J. Biol. Chem. 276, 26622-26628
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