Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.

ABSTRACT: Inside-out and outside-in activations of integrin both play important roles in adhesion formation and cell motility. While such mechanisms of RGD-binding integrin, including integrin β1 and β3, are well documented, mechanosensitive regulations of integrin β6 remain largely unknown. Using traction force-free RGD-membrane as the model system, integrin β6 and viscous RGD ligands initially colocalize, assemble micrometer-sized clusters (15-min), and then gradually dissipate (60-min). Domain-swapping approaches are used and find that integrin β6 chimera with integrin β1's cytoplasmic tail can establish the persistent spatial clustering, suggesting the involvement of inside-out signaling. In vitro, pulldown and microscale thermophoresis experiments reveal that cytoplasmic adapter kindlin2 is the

SUBMITTER: Lee WN 

PROVIDER: S-EPMC12407373 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature