Receptors for 2 different extracellular matrix proteins use the GPVI/FcRγ chain complex for signal transduction. Upon binding of laminin to integrin α6β1 (blue, left) or of collagen to integrin α2β1 (pink, right), tyrosine residues within the ITAMs of the FcRγ chain signaling subunit of the GPVI/FcRγ chain complex become phosphorylated, recruit the Syk tyrosine kinase, and assemble a signaling complex that activates phospholipase Cγ2 (PLCγ2). Activation of PLCγ2 ultimately results in cytokskeletal changes, granule secretion, and activation of cell-surface integrins involved in platelet-matrix and platelet-platelet interactions. This pathway was previously thought to operate exclusively in response to collagen and collagen-related snake venom peptides.