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Crk was first isolated as the v- crk oncogene from chicken retroviruses CT10 and ASV-1. All human cell lines examined to date express a 40 kDa Crk protein. In addition, there is variable expression of 42 kDa and 28 kDa Crk proteins. The c- crk gene is one of a class of genes, such as Nck and GRB2/ASH , which encode proteins that consist mainly of SH2 and SH3 domains. These proteins function as adaptor molecules in tyrosine kinase signal transduction pathways. The SH2 domains interact with phosphotyrosine-containing peptides, while the SH3 domains can enhance this interaction and/or bind to other cellular components. Both the SH2 and SH3 domains of the human Crk protein are required for differentiation of PC12 cells. Thus, Crk has a role in an NGF-induced signaling pathway that involves activation of p21ras. Furthermore, three proteins of 118 kDa, 125 kDa, and 136 kDa which specifically bind to the Crk SH3 domain have been identified.
