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Publication : Integrins β1 and β3 exhibit distinct dynamic nanoscale organizations inside focal adhesions.

First Author  Rossier O Year  2012
Journal  Nat Cell Biol Volume  14
Issue  10 Pages  1057-67
PubMed ID  23023225 Mgi Jnum  J:193934
Mgi Id  MGI:5469937 Doi  10.1038/ncb2588
Citation  Rossier O, et al. (2012) Integrins beta1 and beta3 exhibit distinct dynamic nanoscale organizations inside focal adhesions. Nat Cell Biol 14(10):1057-67
abstractText  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 beta3-integrins are enriched and stationary within FAs, whereas immobilized beta1-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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