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Journal Article

beta(1)- and alpha(v)-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78634

Schiller,  Herbert B.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78097

Hermann,  Michaela-Rosemarie
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78521

Polleux,  Julien
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78917

Zanivan,  Sara
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78772

Sun,  Zhiqi
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78534

Raducanu,  Aurelia
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78356

Mann,  Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77945

Fässler,  Reinhard
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Schiller, H. B., Hermann, M.-R., Polleux, J., Vignaud, T., Zanivan, S., Friedel, C. C., et al. (2013). beta(1)- and alpha(v)-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. NATURE CELL BIOLOGY, 15(6), 625-636. doi:10.1038/ncb2747.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-FCE7-F
Abstract
How different integrins that bind to the same type of extracellular matrix protein mediate specific functions is unclear. We report the functional analysis of beta(1)- and alpha(v)-class integrins expressed in pan-integrin-null fibroblasts seeded on fibronectin. Reconstitution with beta(1)-class integrins promotes myosin-II-independent formation of small peripheral adhesions and cell protrusions, whereas expression of alpha(v)-class integrins induces the formation of large focal adhesions. Co-expression of both integrin classes leads to full myosin activation and traction-force development on stiff fibronectin-coated substrates, with alpha(v)-class integrins accumulating in adhesion areas exposed to high traction forces. Quantitative proteomics linked alpha v-class integrins to a GEF-H1-RhoA pathway coupled to the formin mDia1 but not myosin II, and alpha(5)beta(1) integrins to a RhoA-Rock-myosin II pathway. Our study assigns specific functions to distinct fibronectin-binding integrins, demonstrating that alpha(5)beta(1) integrins accomplish force generation, whereas alpha(v)-class integrins mediate the structural adaptations to forces, which cooperatively enable cells to sense the rigidity of fibronectin-based microenvironments.