β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments

Research output: Contribution to journal › Journal article › Research

Standard

β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. / Schiller, Herbert B; Hermann, Michaela-Rosemarie; Polleux, Julien; Vignaud, Timothée; Zanivan, Sara; Friedel, Caroline C; Sun, Zhiqi; Raducanu, Aurelia; Gottschalk, Kay-E; Théry, Manuel; Mann, Matthias; Fässler, Reinhard.

In: Nature Cell Biology, Vol. 15, No. 6, 06.2013, p. 625-36.

Research output: Contribution to journal › Journal article › Research

Harvard

Schiller, HB, Hermann, M-R, Polleux, J, Vignaud, T, Zanivan, S, Friedel, CC, Sun, Z, Raducanu, A, Gottschalk, K-E, Théry, M, Mann, M & Fässler, R 2013, 'β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments', Nature Cell Biology, vol. 15, no. 6, pp. 625-36. https://doi.org/10.1038/ncb2747

APA

Schiller, H. B., Hermann, M-R., Polleux, J., Vignaud, T., Zanivan, S., Friedel, C. C., Sun, Z., Raducanu, A., Gottschalk, K-E., Théry, M., Mann, M., & Fässler, R. (2013). β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nature Cell Biology, 15(6), 625-36. https://doi.org/10.1038/ncb2747

Vancouver

Schiller HB, Hermann M-R, Polleux J, Vignaud T, Zanivan S, Friedel CC et al. β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nature Cell Biology. 2013 Jun;15(6):625-36. https://doi.org/10.1038/ncb2747

Author

Schiller, Herbert B ; Hermann, Michaela-Rosemarie ; Polleux, Julien ; Vignaud, Timothée ; Zanivan, Sara ; Friedel, Caroline C ; Sun, Zhiqi ; Raducanu, Aurelia ; Gottschalk, Kay-E ; Théry, Manuel ; Mann, Matthias ; Fässler, Reinhard. / β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. In: Nature Cell Biology. 2013 ; Vol. 15, No. 6. pp. 625-36.

Bibtex

@article{6bf55997f9804c068cf8102479338795,
title = "β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments",
abstract = "How different integrins that bind to the same type of extracellular matrix protein mediate specific functions is unclear. We report the functional analysis of β1- and αv-class integrins expressed in pan-integrin-null fibroblasts seeded on fibronectin. Reconstitution with β1-class integrins promotes myosin-II-independent formation of small peripheral adhesions and cell protrusions, whereas expression of αv-class integrins induces the formation of large focal adhesions. Co-expression of both integrin classes leads to full myosin activation and traction-force development on stiff fibronectin-coated substrates, with αv-class integrins accumulating in adhesion areas exposed to high traction forces. Quantitative proteomics linked αv-class integrins to a GEF-H1-RhoA pathway coupled to the formin mDia1 but not myosin II, and α5β1 integrins to a RhoA-Rock-myosin II pathway. Our study assigns specific functions to distinct fibronectin-binding integrins, demonstrating that α5β1integrins accomplish force generation, whereas αv-class integrins mediate the structural adaptations to forces, which cooperatively enable cells to sense the rigidity of fibronectin-based microenvironments.",
keywords = "Animals, Antigens, CD29, Carrier Proteins, Cell Adhesion, Cell Line, Cell Movement, Cellular Microenvironment, Extracellular Matrix, Extracellular Matrix Proteins, Fibroblasts, Fibronectins, Focal Adhesions, Guanine Nucleotide Exchange Factors, Integrin alpha5beta1, Integrin alphaV, Male, Mice, Mice, Transgenic, Myosin Type II, Protein Binding, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, RNA Interference, RNA, Small Interfering, rho-Associated Kinases, rhoA GTP-Binding Protein",
author = "Schiller, {Herbert B} and Michaela-Rosemarie Hermann and Julien Polleux and Timoth{\'e}e Vignaud and Sara Zanivan and Friedel, {Caroline C} and Zhiqi Sun and Aurelia Raducanu and Kay-E Gottschalk and Manuel Th{\'e}ry and Matthias Mann and Reinhard F{\"a}ssler",
year = "2013",
month = jun,
doi = "10.1038/ncb2747",
language = "English",
volume = "15",
pages = "625--36",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "nature publishing group",
number = "6",

}

RIS

TY - JOUR

T1 - β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments

AU - Schiller, Herbert B

AU - Hermann, Michaela-Rosemarie

AU - Polleux, Julien

AU - Vignaud, Timothée

AU - Zanivan, Sara

AU - Friedel, Caroline C

AU - Sun, Zhiqi

AU - Raducanu, Aurelia

AU - Gottschalk, Kay-E

AU - Théry, Manuel

AU - Mann, Matthias

AU - Fässler, Reinhard

PY - 2013/6

Y1 - 2013/6

N2 - How different integrins that bind to the same type of extracellular matrix protein mediate specific functions is unclear. We report the functional analysis of β1- and αv-class integrins expressed in pan-integrin-null fibroblasts seeded on fibronectin. Reconstitution with β1-class integrins promotes myosin-II-independent formation of small peripheral adhesions and cell protrusions, whereas expression of αv-class integrins induces the formation of large focal adhesions. Co-expression of both integrin classes leads to full myosin activation and traction-force development on stiff fibronectin-coated substrates, with αv-class integrins accumulating in adhesion areas exposed to high traction forces. Quantitative proteomics linked αv-class integrins to a GEF-H1-RhoA pathway coupled to the formin mDia1 but not myosin II, and α5β1 integrins to a RhoA-Rock-myosin II pathway. Our study assigns specific functions to distinct fibronectin-binding integrins, demonstrating that α5β1integrins accomplish force generation, whereas αv-class integrins mediate the structural adaptations to forces, which cooperatively enable cells to sense the rigidity of fibronectin-based microenvironments.

AB - How different integrins that bind to the same type of extracellular matrix protein mediate specific functions is unclear. We report the functional analysis of β1- and αv-class integrins expressed in pan-integrin-null fibroblasts seeded on fibronectin. Reconstitution with β1-class integrins promotes myosin-II-independent formation of small peripheral adhesions and cell protrusions, whereas expression of αv-class integrins induces the formation of large focal adhesions. Co-expression of both integrin classes leads to full myosin activation and traction-force development on stiff fibronectin-coated substrates, with αv-class integrins accumulating in adhesion areas exposed to high traction forces. Quantitative proteomics linked αv-class integrins to a GEF-H1-RhoA pathway coupled to the formin mDia1 but not myosin II, and α5β1 integrins to a RhoA-Rock-myosin II pathway. Our study assigns specific functions to distinct fibronectin-binding integrins, demonstrating that α5β1integrins accomplish force generation, whereas αv-class integrins mediate the structural adaptations to forces, which cooperatively enable cells to sense the rigidity of fibronectin-based microenvironments.

KW - Animals

KW - Antigens, CD29

KW - Carrier Proteins

KW - Cell Adhesion

KW - Cell Line

KW - Cell Movement

KW - Cellular Microenvironment

KW - Extracellular Matrix

KW - Extracellular Matrix Proteins

KW - Fibroblasts

KW - Fibronectins

KW - Focal Adhesions

KW - Guanine Nucleotide Exchange Factors

KW - Integrin alpha5beta1

KW - Integrin alphaV

KW - Male

KW - Mice

KW - Mice, Transgenic

KW - Myosin Type II

KW - Protein Binding

KW - Protein-Serine-Threonine Kinases

KW - Proto-Oncogene Proteins

KW - RNA Interference

KW - RNA, Small Interfering

KW - rho-Associated Kinases

KW - rhoA GTP-Binding Protein

U2 - 10.1038/ncb2747

DO - 10.1038/ncb2747

M3 - Journal article

C2 - 23708002

VL - 15

SP - 625

EP - 636

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 6

ER -

ID: 88583486