Metavinculin modulates force transduction in cell adhesion sites

Verena Kanoldt, Carleen Kluger, Christiane Barz, Anna-Lena Schweizer, Deepak Ramanujam, Lukas Windgasse, Stefan Engelhardt, Anna Chrostek-Grashoff and Carsten Grashoff ()
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Verena Kanoldt: Institute of Molecular Cell Biology, University of Münster
Carleen Kluger: Max Planck Institute of Biochemistry, Group of Molecular Mechanotransduction
Christiane Barz: Max Planck Institute of Biochemistry, Group of Molecular Mechanotransduction
Anna-Lena Schweizer: Institute of Molecular Cell Biology, University of Münster
Deepak Ramanujam: Technical University of Munich
Lukas Windgasse: Institute of Molecular Cell Biology, University of Münster
Stefan Engelhardt: Technical University of Munich
Anna Chrostek-Grashoff: Institute of Molecular Cell Biology, University of Münster
Carsten Grashoff: Institute of Molecular Cell Biology, University of Münster

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Vinculin is a ubiquitously expressed protein, crucial for the regulation of force transduction in cells. Muscle cells express a vinculin splice-isoform called metavinculin, which has been associated with cardiomyopathies. However, the molecular function of metavinculin has remained unclear and its role for heart muscle disorders undefined. Here, we have employed a set of piconewton-sensitive tension sensors to probe metavinculin mechanics in cells. Our experiments reveal that metavinculin bears higher molecular forces but is less frequently engaged as compared to vinculin, leading to altered force propagation in cell adhesions. In addition, we have generated knockout mice to investigate the consequences of metavinculin loss in vivo. Unexpectedly, these animals display an unaltered tissue response in a cardiac hypertrophy model. Together, the data reveal that the transduction of cell adhesion forces is modulated by expression of metavinculin, yet its role for heart muscle function seems more subtle than previously thought.

Date: 2020
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DOI: 10.1038/s41467-020-20125-z

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