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CLEC-2 is a member of new family of C-type lectin receptors characterized by a cytosolic YXXL downstream of three acidic amino acids in a sequence known as a hemITAM (hemi-immunoreceptor tyrosine-based activation motif). Dimerization of two phosphorylated CLEC-2 molecules leads to recruitment of the tyrosine kinase Syk via its tandem SH2 domains and initiation of a downstream signaling cascade. Using Syk-deficient and Zap-70-deficient cell lines we show that hemITAM signaling is restricted to Syk and that the upstream triacidic amino acid sequence is required for signaling. Using surface plasmon resonance and phosphorylation studies, we demonstrate that the triacidic amino acids are required for phosphorylation of the YXXL. These results further emphasize the distinct nature of the proximal events in signaling by hemITAM relative to ITAM receptors.


Journal article


J Biol Chem

Publication Date





5127 - 5135


Amino Acid Sequence, Amino Acids, Blood Platelets, Cytosol, Humans, Intracellular Signaling Peptides and Proteins, Kinetics, Lectins, C-Type, Membrane Glycoproteins, Models, Biological, Molecular Sequence Data, Phosphorylation, Protein-Tyrosine Kinases, Sequence Homology, Amino Acid, Signal Transduction, Surface Plasmon Resonance, Syk Kinase, Tyrosine, Viper Venoms, ZAP-70 Protein-Tyrosine Kinase