Breast cancer anti-estrogen resistance protein 3 (BCAR3) is an SH2-containing signal transducer that regulates the proliferation in breast cancer cells []. BCAR3 binds to the adaptor molecule p130Cas (also known as BCAR1), which function as key signalling nodes with important regulatory roles in normal and pathological cells []. BCAR3 promotes cell motility by regulating actin cytoskeletal and adhesion remodeling in invasive breast cancer cells []. It also promotes interactions between p130Cas and the protein tyrosine kinase c-Src, leading to increased c-Src kinase activity and p130Cas phosphorylation [].
Breast cancer anti-estrogen resistance protein 3 (BCAR3) is an SH2-containing signal transducer that regulates the proliferation in breast cancer cells []. BCAR3 binds to the adaptor molecule p130Cas (also known as BCAR1), which function as key signalling nodes with important regulatory roles in normal and pathological cells []. BCAR3 promotes cell motility by regulating actin cytoskeletal and adhesion remodeling in invasive breast cancer cells []. It also promotes interactions between p130Cas and the protein tyrosine kinase c-Src, leading to increased c-Src kinase activity and p130Cas phosphorylation [].This entry represents the SH2 domain found in SHEP1 (also known as SH2D3C), BCAR3 and NSP1 (also known as SH2D3A). SHEP1, BCAR3 and NSP1 are cytoplasmic proteins involved in cell adhesion/migration and antiestrogen resistance. All three proteins contain an SH2 domain and an exchange factor-like domain that binds both Ras GTPases and the scaffolding protein Cas []. In general, SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [].
