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Regulation of protein tyrosine kinases in platelets
E A Clark1, S J Shattil, J S Brugge
1ARIAD Pharmaceuticals Inc., Cambridge, MA 02139.
Trends in Biochemical Sciences
|November 1, 1994
Abstract:
Platelet activation is accompanied by a dramatic increase in tyrosine phosphorylation of many cellular proteins. Phosphorylation of these proteins occurs in successive waves during the activation process, suggesting that several distinct mechanisms, occurring in a temporal order, regulate protein tyrosine kinases and/or phosphatases in activated platelets. Several tyrosine kinases, including Src family kinases, Syk and FAK, have been implicated in these phosphorylation events. These kinases are regulated by distinct receptor-mediated events involving activation of their catalytic activity and alterations in their cellular localization.