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. Author manuscript; available in PMC: 2010 May 15.
Published in final edited form as: J Cell Physiol. 2009 Apr;219(1):45–56. doi: 10.1002/jcp.21649

Figure 8.

Figure 8

Schematic representation of proposed signaling via Pyk2/p130Cas/BCAR3/Rap1 cascade. Pyk2 is constitutively bound to p130Cas through Cas amino-terminal SH3 domain. Carboxy-terminal GEF-like domain (GLD) of BCAR3 interacts with carboxy-terminal p130Cas. ET-1 triggers recruitment of Src to Pyk2 resulting in activation of Src and Pyk2 tyrosine kinase activities. Consequently, p130Cas becomes Tyr phosphorylated and progressively more associates with BCAR3, which causes GTP-loading of Rap1 followed by changes in actin cytoskeleton, cell adhesion and spreading. Whether SH2 domain of BCAR3 plays role in increase of endogenous BCAR3 binding to p130Cas in ET-1 treated cells remains to be determined. It also remains to be established whether BCAR3 is acting itself as a GDP exchange factor for Rap1, or operates via another GEF.