TY - JOUR
T1 - Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways.
AU - Pawson, T.
AU - Olivier, P.
AU - Rozakis-Adcock, M.
AU - McGlade, J.
AU - Henkemeyer, M.
PY - 1993/6/29
Y1 - 1993/6/29
N2 - 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.
AB - 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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U2 - 10.1098/rstb.1993.0069
DO - 10.1098/rstb.1993.0069
M3 - Review article
C2 - 8103930
AN - SCOPUS:0027925812
SN - 0962-8436
VL - 340
SP - 279
EP - 285
JO - Philosophical transactions of the Royal Society of London. Series B, Biological sciences
JF - Philosophical transactions of the Royal Society of London. Series B, Biological sciences
IS - 1293
ER -