Figure 1.

Signal transduction pathway mediated through C‐type lectin‐like receptor 2 (CLEC‐2). Upon CLEC‐2 clustering by rhodocytin, a tyrosine residue in hemi‐ITAM (immunoreceptor tyrosine‐based activation motif) is phosphorylated by the Src family kinase, followed by binding of spleen tyrosine kinase (Syk) to the phosphorylated hemi‐ITAM with its SH2 domain. This binding results in activation of Syk, leading to phosphorylation of the downstream adaptor proteins, LAT and SLP76, and phosphorylation/activation of the downstream tyrosine kinase Btk and phospholipase Cγ2 (PLCγ2). PLCγ2 activation generates of inositol trisphosphate (IP3) and diacylglycerol, resulting in subsequent Ca²⁺ mobilization and protein kinase C (PKC) activation. Intracellular Ca²⁺ mobilization and PKC activate integrin αIIbβ3, which leads to fibrinogen binding and platelet aggregation. pY, phosphorylated tyrosine