αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin

Mitasha Bharadwaj, Nico Strohmeyer, Georgina P. Colo, Jonne Helenius, Niko Beerenwinkel, Herbert B. Schiller, Reinhard Fässler and Daniel J. Müller ()
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Mitasha Bharadwaj: Eidgenössische Technische Hochschule (ETH) Zurich
Nico Strohmeyer: Eidgenössische Technische Hochschule (ETH) Zurich
Georgina P. Colo: Max Planck Institute of Biochemistry
Jonne Helenius: Eidgenössische Technische Hochschule (ETH) Zurich
Niko Beerenwinkel: Eidgenössische Technische Hochschule (ETH) Zurich
Herbert B. Schiller: Max Planck Institute of Biochemistry
Reinhard Fässler: Max Planck Institute of Biochemistry
Daniel J. Müller: Eidgenössische Technische Hochschule (ETH) Zurich

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract Upon binding to the extracellular matrix protein, fibronectin, αV-class and α5β1 integrins trigger the recruitment of large protein assemblies and strengthen cell adhesion. Both integrin classes have been functionally specified, however their specific roles in immediate phases of cell attachment remain uncharacterized. Here, we quantify the adhesion of αV-class and/or α5β1 integrins expressing fibroblasts initiating attachment to fibronectin (≤120 s) by single-cell force spectroscopy. Our data reveals that αV-class integrins outcompete α5β1 integrins. Once engaged, αV-class integrins signal to α5β1 integrins to establish additional adhesion sites to fibronectin, away from those formed by αV-class integrins. This crosstalk, which strengthens cell adhesion, induces α5β1 integrin clustering by RhoA/ROCK/myosin-II and Arp2/3-mediated signalling, whereas overall cell adhesion depends on formins. The dual role of both fibronectin-binding integrin classes commencing with an initial competition followed by a cooperative crosstalk appears to be a basic cellular mechanism in assembling focal adhesions to the extracellular matrix.

Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14348

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DOI: 10.1038/ncomms14348

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