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dc.contributor.authorWatson, A.
dc.contributor.authorChristou, C.
dc.contributor.authorJames, J.
dc.contributor.authorFenton-May, A.
dc.contributor.authorMoncayo, G.
dc.contributor.authorMistry, A.
dc.contributor.authorDavis, S.
dc.contributor.authorGilbert, R.
dc.contributor.authorChakera, Aron
dc.contributor.authorO'Callaghan, C.
dc.identifier.citationWatson, A. and Christou, C. and James, J. and Fenton-May, A. and Moncayo, G. and Mistry, A. and Davis, S. et al. 2009. The platelet receptor CLEC-2 is active as a dimer. Biochemistry. 48 (46): pp. 10988-10996.

The platelet receptor CLEC-2 binds to the snake venom toxin rhodocytin and the tumor cell surface protein podoplanin. Binding of either of these ligands promotes phosphorylation of a single tyrosine residue in the YXXL motif in the intracellular domain of CLEC-2. Phosphorylation of this tyrosine initiates binding of spleen tyrosine kinase (Syk) and triggers further downstream signaling events and ultimately potent platelet activation and aggregation. However, it is unclear how a single YXXL motif can interact efficiently with Syk, which usually recognizes two tandem YXXL repeats presented as an immunoreceptor tyrosine-based activation motif (ITAM). Using bioluminescence resonance energy transfer, coimmuno-preciptitation, recombinant protein expression and analytical gel filtration chromatography, surface plasmon resonance, Western blotting, multiangle light scattering (MALS), and analytical ultracentrifugation, we show that CLEC-2 exists as a non-disulfide-linked homodimer which could alloweach Syk molecule to interact with two YXXL motifs, one from each CLEC-2 monomer. © 2009 American Chemical Society.

dc.publisherAmerican Chemical Society
dc.titleThe platelet receptor CLEC-2 is active as a dimer
dc.typeJournal Article
curtin.departmentCurtin Medical School
curtin.accessStatusFulltext not available

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