RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation.
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.
Mesh Terms:
Alternative Splicing, Animals, Cell Line, Tumor, Cell Membrane, GTP-Binding Proteins, Humans, Lectins, C-Type, Membrane Glycoproteins, Mice, Neoplasm Proteins, Proteasome Endopeptidase Complex, Protein Stability, Receptors for Activated C Kinase, Receptors, Cell Surface, Two-Hybrid System Techniques, Ubiquitin
Alternative Splicing, Animals, Cell Line, Tumor, Cell Membrane, GTP-Binding Proteins, Humans, Lectins, C-Type, Membrane Glycoproteins, Mice, Neoplasm Proteins, Proteasome Endopeptidase Complex, Protein Stability, Receptors for Activated C Kinase, Receptors, Cell Surface, Two-Hybrid System Techniques, Ubiquitin
Biochem Biophys Res Commun
Date: Dec. 11, 2009
PubMed ID: 19785988
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