During platelet activation, receptor-coupled phospholipid hydrolysis stimulates protein kinase C (PKC) and results in the phosphorylation of several proteins, the most prominent being pleckstrin. Pleckstrin is composed of two repeated domains, now called pleckstrin homology (PH) domains, separated by a spacer region that contains several consensus PKC phosphorylation sites. To determine the role of PKC-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in COS cells. Phosphorylation was found to occur almost exclusively on Ser-113 and Ser-117 within the sequence 108-KFARKS*TRRS*IRL-120. Phosphorylation of these sites was confirmed by phosphorylation of the corresponding wild-type and mutant synthetic peptides in vitro.
Research Article| March 15 1996
Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein kinase C
Karen L. CRAIG;
Karen L. CRAIG *
1Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada L8N 3Z5
*To whom correspondence should be addressed at Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Rm 988, Toronto, Ontario, Canada M5G 1X5.
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Biochem J (1996) 314 (3): 937–942.
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Karen L. CRAIG, Calvin B. HARLEY; Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein kinase C. Biochem J 15 March 1996; 314 (3): 937–942. doi: https://doi.org/10.1042/bj3140937
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