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Regulation of the pp72syk protein tyrosine kinase by platelet integrin αIIbβ3

pp72syk is essential for development and function of several hematopoietic cells, and it becomes activated through tandem SH2 interaction with ITAM motifs in immune response receptors. Since Syk is also activated through integrins, which do not contain ITAMs, a CHO cell model system was used to study Syk activation by the platelet integrin, αIIbβ3. As in platelets, Syk underwent tyrosine phosphorylation and activation during CHO cell adhesion to αIIbβ3 ligands, including fibrinogen. This involved Syk autophosphorylation and the tyrosine kinase activity of Src, and it exhibited two novel features. Firstly, unlike αIIbβ3‐mediated activation of pp125FAK, Syk activation could be triggered by the binding of soluble fibrinogen and abolished by truncation of the αIIb or β3 cytoplasmic tail, and it was resistant to inhibition by cytochalasin D. Secondly, it did not require phosphorylated ITAMs since it was unaffected by disruption of an ITAM‐interaction motif in the SH2(C) domain of Syk or by simultaneous overexpression of the tandem SH2 domains. These studies demonstrate that Syk is a proximal component in αIIbβ3 signaling and is regulated as a consequence of intimate functional relationships with the αIIbβ3 cytoplasmic tails and with Src or a closely related kinase. Furthermore, there are fundamental differences in the activation of Syk by αIIbβ3 and immune response receptors, suggesting a unique role for integrins in Syk function.