The Platelet Receptor CLEC-2 Is Active as a Dimer

• Published in: Biochemistry (Easton) Vol. 48; no. 46; pp. 10988 - 10996
• Main Authors: 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, O’Callaghan, Chris A
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 24.11.2009
• Subjects: Cell Line; Cell Membrane - metabolism; Chromatography, Gel; Cystine - analysis; Cystine - chemistry; Fluorescence Resonance Energy Transfer; Humans; Immunoprecipitation; Jurkat Cells; Lectins, C-Type - chemistry; Lectins, C-Type - genetics; Lectins, C-Type - metabolism; Light; Mass Spectrometry; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Molecular Dynamics Simulation; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - metabolism; Protein Binding - physiology; Protein Multimerization - physiology; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; RNA Interference; Scattering, Radiation; Surface Plasmon Resonance; Transfection; Ultracentrifugation; Viper Venoms - chemistry

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 ini...