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Force-independent interactions of talin and vinculin govern integrin-mediated mechanotransduction

Paul Atherton, Franziska Lausecker, Alexandre Carisey, Andrew Gilmore, David Critchley, Igor Barsukov, Christoph Ballestrem
doi: https://doi.org/10.1101/629683
Paul Atherton
1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
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Franziska Lausecker
1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
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Alexandre Carisey
1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
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Andrew Gilmore
1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
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David Critchley
2Department of Biochemistry, University of Leicester, Lancaster Road, Leicester LE1 9HN, UK.
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Igor Barsukov
3Institute of Integrative Biology, University of Liverpool, BioSciences Building, Crown Street, Liverpool L69 7ZB, UK.
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Christoph Ballestrem
1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
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  • For correspondence: christoph.ballestrem@manchester.ac.uk
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Abstract

Talin, vinculin and paxillin are core components of the dynamic link between integrins and actomyosin. Here we study the mechanisms that mediate their activation and association using a mitochondrial-targeting assay, structure-based mutants, and advanced microscopy. As expected, full-length vinculin and talin are auto-inhibited and do not interact with each other in this state. Contrary to previous models that propose a critical role for forces driving talin-vinculin association, our data show that force-independent relief of auto-inhibition is sufficient to mediate their tight interaction. Interestingly, paxillin can bind to both talin and vinculin when either is inactive. Further experiments demonstrate that adhesions containing paxillin and vinculin can form without talin following integrin activation. However, these are largely deficient in exerting traction forces to the matrix. Our observations lead to a model whereby paxillin contributes to talin and vinculin recruitment into nascent adhesions. Activation of the talin-vinculin axis subsequently leads to the engagement with the traction force-machinery and focal adhesion maturation.

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Posted May 07, 2019.
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Force-independent interactions of talin and vinculin govern integrin-mediated mechanotransduction
Paul Atherton, Franziska Lausecker, Alexandre Carisey, Andrew Gilmore, David Critchley, Igor Barsukov, Christoph Ballestrem
bioRxiv 629683; doi: https://doi.org/10.1101/629683
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Force-independent interactions of talin and vinculin govern integrin-mediated mechanotransduction
Paul Atherton, Franziska Lausecker, Alexandre Carisey, Andrew Gilmore, David Critchley, Igor Barsukov, Christoph Ballestrem
bioRxiv 629683; doi: https://doi.org/10.1101/629683

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