Phosphorylation of BCAR1 by SRC-PTK2 complex

SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to enhanced tyrosine phosphorylation of BCAR1 at multiple sites. The Cas substrate domain contains 15 separate YxxP motifs, a main site of tyrosine phosphorylation on the BCAR1 molecule. Once phosphorylated, this domain serves as a docking site for the SH2 domains of CRK or NCK adaptor proteins that affect the downstream MAPK signalling pathway, resulting in cell survival and increased motility.

SH3介导的BCAR1/p130Cas与PTK2的结合与BCAR1在多个位点的酪氨酸磷酸化增强密切相关。Cas底物结构域包含15个独立的YxxP基序，这是BCAR1分子上酪氨酸磷酸化的主要位点。一旦磷酸化，该结构域便充当CRK或NCK适配蛋白SH2结构域的结合位点，这些蛋白影响下游的MAPK信号通路，从而促进细胞存活和增强细胞迁移能力。