de.mpg.escidoc.pubman.appbase.FacesBean
Deutsch
 
Hilfe Wegweiser Impressum Kontakt Einloggen
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

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

MPG-Autoren
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;

Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0013-FCE7-F
Zusammenfassung
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.