THE ROLE OF TENSIN AND FAK INTERACTION IN CELL-MMATRIX ADHESIONS

Abstract

Cell-matrix adhesion complexes are integrin-containing mechanical links between intracellular actin filaments and extracellular matrix. The function of these adhesions is to dynamically sense the substrate environment and convey the information through signaling cascade to the cell. Tensin is one of the main scaffold proteins in adhesions and was believed to play a role at late adhesive structures. Our study showed that tensin3 can localize to both early and late adhesions during cell migration and early cell spreading. The SH2 domain of tensin3 is able to interact with FAK, independent of the phosphorylation state of FAK Tyr397. In FAK-null fibroblasts, assembly of tensin3-rich early adhesions is impaired, and significantly more quantities of tensin3-containing central adhesions are detected. In brief, our study provided a unique insight into the function of FAK on tensin3-rich adhesions. The results imply that FAK is crucial for tensin3 localizations to early adhesions.