CRK monoclonal antibody

CrkII, a cellular homologue of v-Crk, belongs to a family of adaptor proteins with an SH2-SH3-SH3 domain structure that transmits signals from tyrosine kinases. The primary function of Crk is to recruit cytoplasmic proteins in the vicinity of tyrosine kinases through SH2-phospho-tyrosine interaction. Thus, the output from Crk depends on the SH3-binding proteins, which include the C3G and Sos guanine nucleotide exchange proteins, Abl tyrosine kinase, DOCK180 and some STE20-related kinases. The variety of Crk-binding proteins indicates the pleiotropic function of Crk. The two CrkII SH3 domains are separated by a 54 amino acid linker region, which is highly conserved in Xenopus, chicken and mammalian CrkII proteins. Tyrosine 221 in this region is phosphorylated by the Abl tyrosine kinase, IGF-I receptorand EGF receptor. Once Tyr221 is phosphorylated, CrkII undergoes a change in intramolecular folding and SH2-pTyr interaction, which causes rapid dissociation of CrkII from the tyrosine kinase complex.