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Platelet receptors activated via mulitmerization: glycoprotein VI, GPI b‐ IX ‐V, and CLEC ‐2
Author(s) -
Ozaki Y.,
SuzukiInoue K.,
Inoue O.
Publication year - 2013
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/jth.12235
Subject(s) - gpvi , syk , microbiology and biotechnology , signal transduction , receptor , phosphorylation , platelet activation , platelet membrane glycoprotein , ectodomain , chemistry , tyrosine phosphorylation , platelet , cell signaling , biology , tyrosine kinase , biochemistry , immunology
Summary While very different in structure, GPVI – the major collagen receptor on platelet membranes, the GPI b‐ IX ‐V complex – the receptor for von Willebrand factor, and CLEC ‐2, a novel platelet activation receptor for podoplanin, share several common features in terms of function and platelet activation signal transduction pathways. All employ Src family kinases (SFK), Syk, and other signaling molecules involving tyrosine phosphorylation, similar to those of immunoreceptors for T and B cells. There appear to be overlapping functional roles for these glycoproteins, and in some cases, they can compensate for each other, suggesting a degree of redundancy. New ligands for these receptors are being identified, which broadens their functional relevancy. This is particularly true for CLEC ‐2, whose functions beyond hemostasis are being explored. The common mode of signaling, clustering, and localization to glycosphingolipid‐enriched microdomains ( GEM s) suggest that GEM s are central to signaling function by ligand‐dependent association of these receptors, SFK, Syk, phosphotyrosine phosphatases, and other signaling molecules.