Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac.

@article{Pollitt2010PhosphorylationOC,
  title={Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac.},
  author={Alice Y. Pollitt and Beata Grygielska and Bertrand Leblond and Laurent D{\'e}sir{\'e} and Johannes A Eble and Stephen P. Watson},
  journal={Blood},
  year={2010},
  volume={115 14},
  pages={2938-46}
}
The C-type lectin-like receptor 2 (CLEC-2) activates platelets through Src and Syk tyrosine kinases via a single cytoplasmic YxxL motif known as a hem immunoreceptor tyrosine-based activation motif (hemITAM). Here, we demonstrate using sucrose gradient ultracentrifugation and methyl-beta-cyclodextrin treatment that CLEC-2 translocates to lipid rafts upon ligand engagement and that translocation is essential for hemITAM phosphorylation and signal initiation. HemITAM phosphorylation, but not… CONTINUE READING