Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways.

T. Pawson; P. Olivier; M. Rozakis-Adcock; J. McGlade; M. Henkemeyer

doi:10.1098/rstb.1993.0069

Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways.

T. Pawson, P. Olivier, M. Rozakis-Adcock, J. McGlade, M. Henkemeyer

Research output: Contribution to journal › Review article

48 Scopus citations

Abstract

The targets of receptor protein-tyrosine kinases are characterized by Src homology 2 (SH2) domains, that mediate specific interactions with receptor autophosphorylation sites. SH2-mediated interactions are important for the activation of biochemical signalling pathways in cells stimulated with growth factors. A distinct protein module, the SH3 domain, is frequently found in polypeptides that contain SH2 domains, and is also implicated in controlling protein-protein interactions in signal transduction. Evidence suggesting that SH2 and SH3 domains act synergistically in stimulation of the Ras pathway is discussed.

Original language	English (US)
Pages (from-to)	279-285
Number of pages	7
Journal	Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume	340
Issue number	1293
DOIs	https://doi.org/10.1098/rstb.1993.0069
State	Published - Jun 29 1993

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ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)

Cite this

Pawson, T., Olivier, P., Rozakis-Adcock, M., McGlade, J., & Henkemeyer, M. (1993). Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways. Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 340(1293), 279-285. https://doi.org/10.1098/rstb.1993.0069

Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways. / Pawson, T.; Olivier, P.; Rozakis-Adcock, M.; McGlade, J.; Henkemeyer, M.

In: Philosophical transactions of the Royal Society of London. Series B, Biological sciences, Vol. 340, No. 1293, 29.06.1993, p. 279-285.

Research output: Contribution to journal › Review article

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10.1098/rstb.1993.0069