期刊
NATURE CELL BIOLOGY
卷 14, 期 10, 页码 1057-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2588
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资金
- French Ministry of Research
- CNRS
- ANR grant Nanomotility
- Fondation ARC pour la Recherche sur le Cancer
- Conseil Regional Aquitaine
- Fondation pour la Recherche Medicate
- ERC [232942 Nano-Dyn-Syn, 235552 Glutraf]
- Human Frontiers Science Programme
- Ligue National contre le Cancer-equipe labellisee
Integrins in focal adhesions (FAs) mediate adhesion and force transmission to extracellular matrices essential for cell motility, proliferation and differentiation. Different fibronectin-binding integrins, simultaneously present in FAs, perform distinct functions. Yet, how integrin dynamics control biochemical and biomechanical processes in FAs is still elusive. Using single-protein tracking and super-resolution imaging we revealed the dynamic nano-organizations of integrins and talin inside FAs. Integrins reside in FAs through free-diffusion and immobilization cycles. Integrin activation promotes immobilization, stabilized in FAs by simultaneous connection to fibronectin and actin-binding proteins. Talin is recruited in FAs directly from the cytosol without membrane free-diffusion, restricting integrin immobilization to FAs. Immobilized beta(3)-integrins are enriched and stationary within FAs, whereas immobilized beta(1)-integrins are less enriched and exhibit rearward movements. Talin is enriched and mainly stationary, but also exhibited rearward movements in FAs, consistent with stable connections with both beta-integrins. Thus, differential transmission of actin motion to fibronectin occurs through specific integrins within FAs.
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