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

Rossier, Olivier; Octeau, Vivien; Sibarita, Jean‐Baptiste; Leduc, Cécile; Tessier, Béatrice; Nair, Deepak; Gatterdam, Volker; Destaing, Olivier; Albigès-Rizo, Corinne; Tampé, Robert; Cognet, Laurent; Choquet, Daniel; Lounis, Brahim; Giannone, Grégory

doi:10.1038/ncb2588

Cited by 357 publications

(469 citation statements)

References 70 publications

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“…S3C). Thus, GFP-integrin mobility is constrained in FAs, in agreement with fluorescence recovery after photobleaching and single-molecule analyses (16,17). Next, we analyzed the anisotropy of the αV-GFP-constrained chimera.…”

Section: Resultssupporting

confidence: 66%

Actin retrograde flow actively aligns and orients ligand-engaged integrins in focal adhesions

Swaminathan

Kalappurakkal

Mehta

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

112

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Integrins are transmembrane receptors that, upon activation, bind extracellular ligands and link them to the actin filament (F-actin) cytoskeleton to mediate cell adhesion and migration. Cytoskeletal forces in migrating cells generated by polymerization-or contractilitydriven "retrograde flow" of F-actin from the cell leading edge have been hypothesized to mediate integrin activation for ligand binding. This predicts that these forces should align and orient activated, ligand-bound integrins at the leading edge. Here, polarization-sensitive fluorescence microscopy of GFP-αVβ3 integrins in fibroblasts shows that integrins are coaligned in a specific orientation within focal adhesions (FAs) in a manner dependent on binding immobilized ligand and a talin-mediated linkage to the F-actin cytoskeleton. These findings, together with Rosetta modeling, suggest that integrins in FA are coaligned and may be highly tilted by cytoskeletal forces. Thus, the F-actin cytoskeleton sculpts an anisotropic molecular scaffold in FAs, and this feature may underlie the ability of migrating cells to sense directional extracellular cues.cell migration | mechanosensing | fluorescence polarization microscopy

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Section: Resultssupporting

confidence: 66%

Actin retrograde flow actively aligns and orients ligand-engaged integrins in focal adhesions

Swaminathan

Kalappurakkal

Mehta

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

112

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“…For example, the ubiquitous beta1a‐integrin was recently shown to bind preferentially to talin2 51 whereas the muscle‐specific beta1d‐integrin has a threefold higher preference for talin2 over talin1 33, 52, 53. This provides selectivity for different talin and integrin complexes, and different couplings are likely to regulate different cellular functions 54.…”

Section: Structure Of Talin 1 Andmentioning

confidence: 99%

The tale of two talins – two isoforms to fine‐tune integrin signalling

Gough

Goult

2018

FEBS Letters

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Talins are cytoplasmic adapter proteins essential for integrin‐mediated cell adhesion to the extracellular matrix. Talins control the activation state of integrins, link integrins to cytoskeletal actin, recruit numerous signalling molecules that mediate integrin signalling and coordinate recruitment of microtubules to adhesion sites via interaction with KANK (kidney ankyrin repeat‐containing) proteins. Vertebrates have two talin genes, TLN1 and TLN2. Although talin1 and talin2 share 76% protein sequence identity (88% similarity), they are not functionally redundant, and the differences between the two isoforms are not fully understood. In this Review, we focus on the similarities and differences between the two talins in terms of structure, biochemistry and function, which hint at subtle differences in fine‐tuning adhesion signalling.

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“…Integrin αvβ3 promotes the formation of large adhesion sites (32). In contrast, α5β1 induces the formation of smaller and more dynamic adhesion sites at the cell periphery (32,33) and stronger traction force (32,34). It is also much more efficient than αvβ3 in inducing fibronectin polymerization on the cell surface (35).…”

Section: Integrin Type-specific Signalsmentioning

confidence: 99%

Common and Diverging Integrin Signals Downstream of Adhesion and Mechanical Stimuli and Their Interplay with Reactive Oxygen Species

Zeller

Johansson

2014

Biophys. Rev. Lett.

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The integrin family of adhesion receptors regulates basic functions of cells, and the signals they induce are altered in tumor cells. In this review we discuss how different integrin-dependent signals are generated during cell adhesion and by physical forces acting on cells. We also describe how reactive oxygen species are integral parts of integrin signaling and highlight a few important questions in the field. Answers to those may improve our understanding of integrins and their role in the development of cancer.

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

Cited by 357 publications

References 70 publications

Actin retrograde flow actively aligns and orients ligand-engaged integrins in focal adhesions

Actin retrograde flow actively aligns and orients ligand-engaged integrins in focal adhesions

The tale of two talins – two isoforms to fine‐tune integrin signalling

Common and Diverging Integrin Signals Downstream of Adhesion and Mechanical Stimuli and Their Interplay with Reactive Oxygen Species

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