Integrins beta(1) and beta(3) exhibit distinct dynamic nanoscale organizations inside focal adhesions
Nat Cell Biol. 2012-09-30; 14(10): 1057-1067
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1. Nat Cell Biol. 2012 Oct;14(10):1057-67. doi: 10.1038/ncb2588. Epub 2012 Sep 30.
Integrins β1 and β3 exhibit distinct dynamic nanoscale organizations inside focal
Rossier O(1), Octeau V, Sibarita JB, Leduc C, Tessier B, Nair D, Gatterdam V,
Destaing O, Albigès-Rizo C, Tampé R, Cognet L, Choquet D, Lounis B, Giannone G.
(1)Interdisciplinary Institute for Neuroscience, University of Bordeaux, UMR
5297, F-33000 Bordeaux, France.
Nat Cell Biol. 2012 Nov;14(11):1231.
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 β3-integrins are enriched and stationary within FAs, whereas
immobilized β1-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 β-integrins. Thus, differential
transmission of actin motion to fibronectin occurs through specific integrins
PMID: 23023225 [Indexed for MEDLINE]