Relief of talin auto-inhibition triggers a force-independent association with vinculinCitation formats

  • External authors:
  • Paul Atherton
  • Franziska Lausecker
  • Alexandre Carisey
  • David Critchley
  • Igor Barsukov

Standard

Relief of talin auto-inhibition triggers a force-independent association with vinculin. / Atherton, Paul; Lausecker, Franziska; Carisey, Alexandre; Gilmore, Andrew; Critchley, David; Barsukov, Igor; Ballestrem, Christoph.

In: The Journal of cell biology, Vol. 219, No. 1, e201903134, 05.12.2019.

Research output: Contribution to journalArticlepeer-review

Harvard

Atherton, P, Lausecker, F, Carisey, A, Gilmore, A, Critchley, D, Barsukov, I & Ballestrem, C 2019, 'Relief of talin auto-inhibition triggers a force-independent association with vinculin', The Journal of cell biology, vol. 219, no. 1, e201903134. https://doi.org/10.1083/jcb.201903134

APA

Atherton, P., Lausecker, F., Carisey, A., Gilmore, A., Critchley, D., Barsukov, I., & Ballestrem, C. (2019). Relief of talin auto-inhibition triggers a force-independent association with vinculin. The Journal of cell biology, 219(1), [e201903134]. https://doi.org/10.1083/jcb.201903134

Vancouver

Atherton P, Lausecker F, Carisey A, Gilmore A, Critchley D, Barsukov I et al. Relief of talin auto-inhibition triggers a force-independent association with vinculin. The Journal of cell biology. 2019 Dec 5;219(1). e201903134. https://doi.org/10.1083/jcb.201903134

Author

Atherton, Paul ; Lausecker, Franziska ; Carisey, Alexandre ; Gilmore, Andrew ; Critchley, David ; Barsukov, Igor ; Ballestrem, Christoph. / Relief of talin auto-inhibition triggers a force-independent association with vinculin. In: The Journal of cell biology. 2019 ; Vol. 219, No. 1.

Bibtex

@article{95e7691d35024b5989618b27ef782664,
title = "Relief of talin auto-inhibition triggers a force-independent association with vinculin",
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. However, 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. We also found that paxillin can bind to both talin and vinculin when either is inactive. Further experiments demonstrated 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. ",
keywords = "talin, vinculin, mechano-transduction, Paxillin",
author = "Paul Atherton and Franziska Lausecker and Alexandre Carisey and Andrew Gilmore and David Critchley and Igor Barsukov and Christoph Ballestrem",
year = "2019",
month = dec,
day = "5",
doi = "10.1083/jcb.201903134",
language = "English",
volume = "219",
journal = "The Journal of cell biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "1",

}

RIS

TY - JOUR

T1 - Relief of talin auto-inhibition triggers a force-independent association with vinculin

AU - Atherton, Paul

AU - Lausecker, Franziska

AU - Carisey, Alexandre

AU - Gilmore, Andrew

AU - Critchley, David

AU - Barsukov, Igor

AU - Ballestrem, Christoph

PY - 2019/12/5

Y1 - 2019/12/5

N2 - 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. However, 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. We also found that paxillin can bind to both talin and vinculin when either is inactive. Further experiments demonstrated 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.

AB - 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. However, 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. We also found that paxillin can bind to both talin and vinculin when either is inactive. Further experiments demonstrated 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.

KW - talin

KW - vinculin

KW - mechano-transduction

KW - Paxillin

U2 - 10.1083/jcb.201903134

DO - 10.1083/jcb.201903134

M3 - Article

VL - 219

JO - The Journal of cell biology

JF - The Journal of cell biology

SN - 0021-9525

IS - 1

M1 - e201903134

ER -