Review article
Biomechanical properties of intermediate filaments: from tissues to single filaments and back
Article first published online: 22 DEC 2006
DOI: 10.1002/bies.20514
Copyright © 2006 Wiley Periodicals, Inc.
Additional Information
How to Cite
Kreplak, L. and Fudge, D. (2007), Biomechanical properties of intermediate filaments: from tissues to single filaments and back. Bioessays, 29: 26–35. doi: 10.1002/bies.20514
Publication History
- Issue published online: 22 DEC 2006
- Article first published online: 22 DEC 2006
Funded by
- L.K. was supported by a grant from the Swiss Society for Research on Muscular Diseases awarded to Ueli Aebi and Sergei Strelkov. D.F was supported by a Natural Sciences and Engineering Research Council of Canada postdoctoral fellowship and a Seed Grant for Innovative Projects from the Faculty of Medicine at the University of British Columbia. This work was also supported by grants from the NCCR “Nanoscale Science”, the Swiss National Science Foundation, and the M.E. Müller Foundation, all awarded to Ueli Aebi
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Abstract
The animal cell cytoskeleton consists of three interconnected filament systems: actin-containing microfilaments (MFs), microtubules (MTs), and the lesser known intermediate filaments (IFs). All IF proteins share a common tripartite domain structure and the ability to assemble into 8–12 nm wide filaments. Electron microscopy data suggest that IFs are built according to a completely different plan from that of MFs and MTs. IFs are known to impart mechanical stability to cells and tissues but, until recently, the biomechanical properties of single IFs were unknown. However, with the discovery of naturally occurring micrometer-wide IF bundles and the development of new methodologies to mechanically probe single filaments, it is now possible to propose a more unified view of IF biomechanics. Unlike MFs and MTs, single IFs can now be described as flexible, extensible and tough, which has important implications for our understanding of cell and tissue mechanics. Furthermore, the molecular mechanisms at play when IFs are deformed point toward a pivotal role for them in mechanotransduction. BioEssays 29: 26–35, 2007. © 2006 Wiley Periodicals, Inc.

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