Distinct focal adhesion protein modules control different aspects of mechanotransductionCitation formats

Standard

Distinct focal adhesion protein modules control different aspects of mechanotransduction. / Stutchbury, Benjamin; Atherton, Paul; Tsang, Ricky; Wang, De-Yao; Ballestrem, Christoph.

In: Journal of Cell Science, Vol. 130, No. 9, 2017, p. 1612-1624.

Research output: Contribution to journalArticle

Harvard

Stutchbury, B, Atherton, P, Tsang, R, Wang, D-Y & Ballestrem, C 2017, 'Distinct focal adhesion protein modules control different aspects of mechanotransduction', Journal of Cell Science, vol. 130, no. 9, pp. 1612-1624. https://doi.org/10.1242/jcs.195362

APA

Stutchbury, B., Atherton, P., Tsang, R., Wang, D-Y., & Ballestrem, C. (2017). Distinct focal adhesion protein modules control different aspects of mechanotransduction. Journal of Cell Science, 130(9), 1612-1624. https://doi.org/10.1242/jcs.195362

Vancouver

Stutchbury B, Atherton P, Tsang R, Wang D-Y, Ballestrem C. Distinct focal adhesion protein modules control different aspects of mechanotransduction. Journal of Cell Science. 2017;130(9):1612-1624. https://doi.org/10.1242/jcs.195362

Author

Stutchbury, Benjamin ; Atherton, Paul ; Tsang, Ricky ; Wang, De-Yao ; Ballestrem, Christoph. / Distinct focal adhesion protein modules control different aspects of mechanotransduction. In: Journal of Cell Science. 2017 ; Vol. 130, No. 9. pp. 1612-1624.

Bibtex

@article{651805a4200e4898b646d650592b709f,
title = "Distinct focal adhesion protein modules control different aspects of mechanotransduction",
abstract = "Focal adhesions (FAs) are macromolecular complexes that regulate cell adhesion and mechanotransduction. Using fluorescence recovery after photobleaching (FRAP) and fluorescence loss after photoactivation (FLAP), we found that the mobility of core FA proteins correlates with protein function. Structural proteins such as tensin, talin and vinculin are significantly less mobile in FAs than signaling proteins such as FAK and paxillin. The mobilities of the structural proteins are directly influenced by substrate stiffness, suggesting they are involved in sensing the rigidity of the extracellular environment. The turnover rates of FAK and paxillin as well as kindlin2 are not influenced by substrate stiffness. By using specific Src and FAK kinase inhibitors, we reveal that force-sensing by vinculin occurs independently of FAK and paxillin phosphorylation. However, this phosphorylation is required for downstream, Rac1-driven cellular processes, such as protrusion and cell migration. Overall, we show that the FA is composed of different functional modules that separately control mechanosensing and the cellular mechano-response.",
keywords = "Vinculin, Talin, Paxillin, FAK, Mechanotransduction, Focal adhesion",
author = "Benjamin Stutchbury and Paul Atherton and Ricky Tsang and De-Yao Wang and Christoph Ballestrem",
year = "2017",
doi = "10.1242/jcs.195362",
language = "English",
volume = "130",
pages = "1612--1624",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "9",

}

RIS

TY - JOUR

T1 - Distinct focal adhesion protein modules control different aspects of mechanotransduction

AU - Stutchbury, Benjamin

AU - Atherton, Paul

AU - Tsang, Ricky

AU - Wang, De-Yao

AU - Ballestrem, Christoph

PY - 2017

Y1 - 2017

N2 - Focal adhesions (FAs) are macromolecular complexes that regulate cell adhesion and mechanotransduction. Using fluorescence recovery after photobleaching (FRAP) and fluorescence loss after photoactivation (FLAP), we found that the mobility of core FA proteins correlates with protein function. Structural proteins such as tensin, talin and vinculin are significantly less mobile in FAs than signaling proteins such as FAK and paxillin. The mobilities of the structural proteins are directly influenced by substrate stiffness, suggesting they are involved in sensing the rigidity of the extracellular environment. The turnover rates of FAK and paxillin as well as kindlin2 are not influenced by substrate stiffness. By using specific Src and FAK kinase inhibitors, we reveal that force-sensing by vinculin occurs independently of FAK and paxillin phosphorylation. However, this phosphorylation is required for downstream, Rac1-driven cellular processes, such as protrusion and cell migration. Overall, we show that the FA is composed of different functional modules that separately control mechanosensing and the cellular mechano-response.

AB - Focal adhesions (FAs) are macromolecular complexes that regulate cell adhesion and mechanotransduction. Using fluorescence recovery after photobleaching (FRAP) and fluorescence loss after photoactivation (FLAP), we found that the mobility of core FA proteins correlates with protein function. Structural proteins such as tensin, talin and vinculin are significantly less mobile in FAs than signaling proteins such as FAK and paxillin. The mobilities of the structural proteins are directly influenced by substrate stiffness, suggesting they are involved in sensing the rigidity of the extracellular environment. The turnover rates of FAK and paxillin as well as kindlin2 are not influenced by substrate stiffness. By using specific Src and FAK kinase inhibitors, we reveal that force-sensing by vinculin occurs independently of FAK and paxillin phosphorylation. However, this phosphorylation is required for downstream, Rac1-driven cellular processes, such as protrusion and cell migration. Overall, we show that the FA is composed of different functional modules that separately control mechanosensing and the cellular mechano-response.

KW - Vinculin

KW - Talin

KW - Paxillin

KW - FAK

KW - Mechanotransduction

KW - Focal adhesion

U2 - 10.1242/jcs.195362

DO - 10.1242/jcs.195362

M3 - Article

VL - 130

SP - 1612

EP - 1624

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 9

ER -