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The platelet receptor CLEC-2 is active as a dimer
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Watson, Aleksandra A., Christou, Charita M., James, John R., Fenton-May, Angharad E., Moncayo, Gerald E., Mistry, Anita R., Davis, Simon J., Gilbert, Robert J. C., Chakera, Aron and O’Callaghan, Chris A. (2009) The platelet receptor CLEC-2 is active as a dimer. Biochemistry, 48 (46). pp. 10988-10996. doi:10.1021/bi901427d
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Official URL: http://dx.doi.org/10.1021/bi901427d
Abstract
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, coimmunopreciptitation, 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 allow each Syk molecule to interact with two YXXL motifs, one from each CLEC-2 monomer.
| Item Type: | Journal Article | ||||||
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| Divisions: | Faculty of Medicine > Warwick Medical School > Biomedical Sciences Faculty of Medicine > Warwick Medical School |
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| Journal or Publication Title: | Biochemistry | ||||||
| Publisher: | American Chemical Society | ||||||
| ISSN: | 0006-2960 | ||||||
| Official Date: | 24 November 2009 | ||||||
| Dates: |
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| Volume: | 48 | ||||||
| Number: | 46 | ||||||
| Page Range: | pp. 10988-10996 | ||||||
| DOI: | 10.1021/bi901427d | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Restricted or Subscription Access |
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