Functional interaction of protein kinase Calpha with the tyrosine kinases Syk and Src in human platelets.

@article{Pula2005FunctionalIO,
  title={Functional interaction of protein kinase Calpha with the tyrosine kinases Syk and Src in human platelets.},
  author={Giordano Pula and David B. Crosby and Julie Baker and Alastair W Poole},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 8},
  pages={7194-205}
}
There is a high degree of cross-talk between tyrosine phosphorylation and the serine/threonine phosphorylation signaling pathways. Here we show a physical and functional interaction between the classical protein kinase C isoform (cPKC), PKCalpha, and two major nonreceptor tyrosine kinases in platelets, Syk and Src. In the presence of the cPKC-selective inhibitor Go6976, platelet 5-hydroxytryptamine release was abolished in response to co-activation of glycoproteins VI and Ib-IX-V by the snake… CONTINUE READING

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