RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation.
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Ruan Y, Guo L, Qiao Y, Hong Y, Zhou L, Sun L, Wang L, Zhu H, Wang L, Yun X, Xie J, Gu J
RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation.
Biochem Biophys Res Commun. 2009 Dec 11;390(2):217-22. doi: 10.1016/j.bbrc.2009.09.087. Epub 2009 Sep 26.
- PubMed ID
- 19785988 [ View in PubMed]
- Abstract
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.