Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways
Tony J. Pawson, Paul Olivier, Maria Rozakis-Adcock, Jane C. McGlade, Mark J. Henkemeyer
Abstract
Tony J. Pawson, Paul Olivier, Maria Rozakis-Adcock, Jane C. McGlade, Mark J. Henkemeyer
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.
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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.
Key concepts: SH2 domain, SH3 domain, Autophosphorylation, Proto-oncogene tyrosine-protein kinase Src, Phosphotyrosine-binding domain, Cell biology, Signal transduction, Receptor tyrosine kinase