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

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.

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 Creators:
Schiller, Herbert B.1, Author              
Hermann, Michaela-Rosemarie1, Author              
Polleux, Julien1, Author              
Vignaud, Timothee2, Author
Zanivan, Sara3, Author              
Friedel, Caroline C.2, Author
Sun, Zhiqi1, Author              
Raducanu, Aurelia1, Author              
Gottschalk, Kay-E.2, Author
Thery, Manuel2, Author
Mann, Matthias3, Author              
Fässler, Reinhard1, Author              
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
2external, ou_persistent22              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: CELL-MATRIX ADHESIONS; ALPHA-V INTEGRINS; FOCAL ADHESIONS; QUANTITATIVE PROTEOMICS; INTERACTION DATABASE; IN-VIVO; KINASE; ALPHA-V-BETA-3; MATURATION; MIGRATION
 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.

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Language(s): eng - English
 Dates: 2013-06
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000319804200013
DOI: 10.1038/ncb2747
 Degree: -

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Title: NATURE CELL BIOLOGY
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 15 (6) Sequence Number: - Start / End Page: 625 - 636 Identifier: ISSN: 1465-7392