Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2022.12.19.521109v1?rss=1

Authors: Kumar, S., Stainer, A., Dubrulle, J., Simpkins, C., Cooper, J.

Abstract:
Integrins link the cytoskeleton to the extracellular matrix for cell movement. Integrin ligation stimulates tyrosine phosphorylation of integrin-associated proteins but the role of phosphorylation signaling in regulating integrin-cytoskeletal linkages and assembly of focal adhesions is unclear. Using spreading or migrating epithelial cells, we provide evidence that phosphorylated Cas (p130Cas, BCAR1), its binding partner, Crk, and inactive focal adhesion kinase (FAK) cluster together with inactive integrins at the cell periphery at sites that develop into focal adhesions containing F-actin, active integrins, active FAK and mechanosensing proteins such as vinculin and talin. Cas, Crk, Src family kinases (SFK) and Rac1 are required for focal adhesion formation and cell spreading, while vinculin is not needed for Cas clustering. Furthermore, Rac1 provides positive feedback onto Cas through reactive oxygen, opposed by negative feedback from the ubiquitin proteasome system. The results suggest that phosphorylation signaling precedes and regulates mechanosensing during focal adhesion formation.

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