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The vimentin cytoskeleton: when polymer physics meets cell biology.

Authors
  • Patteson, Alison E1
  • Carroll, Robert J
  • Iwamoto, Daniel V
  • Janmey, Paul A
  • 1 Physics Department, Syracuse University, Syracuse, NY 13244, USA. BioInspired Institute, Syracuse University, Syracuse, NY 13244, USA.
Type
Published Article
Journal
Physical Biology
Publisher
IOP Publishing
Publication Date
Dec 01, 2020
Volume
18
Issue
1
Pages
11001–11001
Identifiers
DOI: 10.1088/1478-3975/abbcc2
PMID: 32992303
Source
Medline
Language
English
License
Unknown

Abstract

The proper functions of tissues depend on the ability of cells to withstand stress and maintain shape. Central to this process is the cytoskeleton, comprised of three polymeric networks: F-actin, microtubules, and intermediate filaments (IFs). IF proteins are among the most abundant cytoskeletal proteins in cells; yet they remain some of the least understood. Their structure and function deviate from those of their cytoskeletal partners, F-actin and microtubules. IF networks show a unique combination of extensibility, flexibility and toughness that confers mechanical resilience to the cell. Vimentin is an IF protein expressed in mesenchymal cells. This review highlights exciting new results on the physical biology of vimentin intermediate filaments and their role in allowing whole cells and tissues to cope with stress.

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