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Biochem Biophys Res Commun. 2009 Dec 11;390(2):217-22. doi: 10.1016/j.bbrc.2009.09.087. Epub 2009 Sep 26.

RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation.

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  • 1Gene Research Center, Shanghai Medical College of Fudan University, Shanghai 200032, People's Republic of China.


CLEC-2 is a C-type lectin-like receptor and plays an important role in platelet activation. Snake venom toxin rhodocytin and the endogenous sialoglycoprotein podoplanin are identified as ligands for CLEC-2 and function as stimulators in platelet activation. We also previously indentified two splice variants of murine CLEC-2 as well as a soluble fragment cleaved from the full-length form. However, little is known about the interacting partners with the cytoplasmic region of CLEC-2. In this study, we reported that RACK1, the receptor for activated C-kinase 1, associated with the cytoplasmic tail of CLEC-2. Moreover, overexpression of RACK1 decreased the stability of CLEC-2 through promoting its ubiquitin-proteasome degradation, without impairing surface expression and downstream signaling of CLEC-2. Taken together, these results suggest RACK1 as a novel modulator of CLEC-2 expression.

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