mProX™ Human BCAR1 Stable Cell Line

Kumar S, et al. "Cas phosphorylation regulates focal adhesion assembly.." eLife, 2023.
Integrin-mediated cell attachment results in the rapid induction of tyrosine kinase signaling. Despite several years of research, the role of this signaling in integrin activation and focal adhesion assembly remains uncertain. Evidence has been provided that the Src-family kinase (SFK) substrate Cas (Crk-associated substrate, p130Cas, BCAR1) is phosphorylated and bound to its Crk/CrkL effectors in clustered formations, serving as precursors to focal adhesions. These initial phospho-Cas clusters contain the inactive, closed conformation of integrin beta1. Subsequently, as integrin beta1 becomes activated, the levels of phospho-Cas and total Cas decrease, along with the recruitment of core focal adhesion proteins such as vinculin, talin, kindlin, and paxillin. The presence of Cas is crucial for cell spreading and focal adhesion assembly in both epithelial and fibroblast cells on collagen and fibronectin. Formation of Cas clusters requires the presence of Cas, Crk/CrkL, SFKs, and Rac1, but is not dependent on vinculin. The enzyme Rac1 functions to provide positive feedback to Cas through reactive oxygen, while negative feedback is supplied by the ubiquitin proteasome system. These findings propose a two-step model for focal adhesion assembly, in which clusters of phospho-Cas, effectors, and inactive integrin beta1 grow through positive feedback before integrin activation and recruitment of core focal adhesion proteins occur. (80 words)
Pubmed: 37489578   DOI: 10.7554/eLife.90234

Yang B, et al. "Creatine kinase brain-type regulates BCAR1 phosphorylation to facilitate DNA ." iScience, 2023.
The study focuses on the role of creatine kinase (CK) in energy production and its potential non-metabolic functions. CK is responsible for converting creatine and phosphocreatine to replenish ATP for energy needs in the body. In mice, deficiency in CK leads to reduced muscle activity and neurological disorders. By demonstrating a new mechanism, the authors reveal that creatine kinase brain-type (CKB) may act as a protein kinase to regulate BCAR1 Y327 phosphorylation. This enhances the association between BCAR1 and RBBP4, which in turn binds to the promoter region of DNA damage repair gene RAD51 and activates its transcription. This ultimately promotes DNA damage repair and highlights the possible independent role of CKB in this process.
Pubmed: 37182100   DOI: 10.1016/j.isci.2023.106684