Vinculin controls talin engagement with the actomyosin machinery

Paul Atherton, Ben Stutchbury, Wang De-Yao, Devina Jethwa, Ricky Tsang, Eugenia Meiler-Rodriguez, Pengbo Wang, Neil Bate, Roy Zent, Igor L. Barsukov, Benjamin T. Goult, David R. Critchley and Christoph Ballestrem ()
Additional contact information
Paul Atherton: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Ben Stutchbury: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Wang De-Yao: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Devina Jethwa: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Ricky Tsang: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Eugenia Meiler-Rodriguez: Complutense, University of Madrid
Pengbo Wang: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Neil Bate: University of Leicester
Roy Zent: Vanderbilt Centre for Kidney Disease, S-3223 Medical Centre
Igor L. Barsukov: Institute of Integrative Biology, University of Liverpool
Benjamin T. Goult: School of Biosciences, University of Kent
David R. Critchley: University of Leicester
Christoph Ballestrem: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The link between extracellular-matrix-bound integrins and intracellular F-actin is essential for cell spreading and migration. Here, we demonstrate how the actin-binding proteins talin and vinculin cooperate to provide this link. By expressing structure-based talin mutants in talin null cells, we show that while the C-terminal actin-binding site (ABS3) in talin is required for adhesion complex assembly, the central ABS2 is essential for focal adhesion (FA) maturation. Thus, although ABS2 mutants support cell spreading, the cells lack FAs, fail to polarize and exert reduced force on the surrounding matrix. ABS2 is inhibited by the preceding mechanosensitive vinculin-binding R3 domain, and deletion of R2R3 or expression of constitutively active vinculin generates stable force-independent FAs, although cell polarity is compromised. Our data suggest a model whereby force acting on integrin-talin complexes via ABS3 promotes R3 unfolding and vinculin binding, activating ABS2 and locking talin into an actin-binding configuration that stabilizes FAs.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/ncomms10038 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10038

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms10038

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().