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Characterization of Grb2-binding proteins in human platelets activated by
Fc gamma RIIA cross-linking
A Robinson, J Gibbins, B Rodriguez-Linares, PM Finan, L Wilson, S Kellie, P Findell and SP Watson
University Department of Pharmacology, Oxford, UK.
Glutathione-S-transferase (GST)-Grb2 fusion proteins have been used to
identify the potential role of Grb2-binding proteins in platelet activation
by the platelet low-affinity IgG receptor, Fc gamma RIIA. Two tyrosine
phosphoproteins of 38 and 63 kD bind to the SH2 domain of Grb2 following Fc
gamma RIIA stimulation of platelets. Both are located in the particulate
fraction following platelet activation and are also able to bind to a
GST-construct containing the SH2 and SH3 domains of phospholipase C gamma
1. p38 also forms a complex with the tyrosine kinase csk in stimulated
cells and is a substrate for the kinase. The SH3 domains of Grb2 form a
stable complex with SOS1 and two proteins of 75 kD and 120 kD, which
undergo tyrosine phosphorylation in Fc gamma RIIA stimulated cells. The
75-kD protein is recognized by antibodies to SLP-76, which has recently
been isolated from T cells and sequenced. Tyrosine phosphorylation of p38
and p63 is also observed in platelets stimulated by the tyrosine
kinase-linked receptor agonist collagen and by the G protein-coupled
receptor agonist thrombin, although phosphorylation of SLP-76 is only
observed in collagen-stimulated platelets. p38 and p63 may provide a
docking site for Grb2, thereby linking Grb2 SH3-binding proteins SOS1,
SLP-76, and p120 to downstream signalling events.
Volume 88,
Issue 2,
pp. 522-530,
07/15/1996
Copyright © 1996 by The American Society of Hematology
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