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Cited by 440

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Force-Induced Unfolding of Fibronectin in the Extracellular Matrix of Living Cells

Open access
Smith, Michael L, Gourdon, Delphine, Little, William C, Kubow, Kristopher E, Eguiluz, R. Andresen, Luna-Morris, Sheila, Vogel, Viola·2007·PLoS Biology
DOI 10.1371/journal.pbio.0050268
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Abstract

Whether mechanically unfolded fibronectin (Fn) is present within native extracellular matrix fibrils is controversial. Fn extensibility under the influence of cell traction forces has been proposed to originate either from the force-induced lengthening of an initially compact, folded quaternary structure as is found in solution (quaternary structure model, where the dimeric arms of Fn cross each other), or from the force-induced unfolding of type III modules (unfolding model). Clarification of this issue is central to our understanding of the structural arrangement of Fn within fibrils, the mechanism of fibrillogenesis, and whether cryptic sites, which are exposed by partial protein unfolding, can be exposed by cell-derived force. In order to differentiate between these two models, two fluorescence resonance energy transfer schemes to label plasma Fn were applied, with sensitivity to either compact-to-extended conformation (arm separation) without loss of secondary structure or compact-to-unfolded conformation. Fluorescence resonance energy transfer studies revealed that a significant fraction of fibrillar Fn within a three-dimensional human fibroblast matrix is partially unfolded. Complete relaxation of Fn fibrils led to a refolding of Fn. The compactly folded quaternary structure with crossed Fn arms, however, was never detected within extracellular matrix fibrils. We conclude that the resting state of Fn fibrils does not contain Fn molecules with crossed-over arms, and that the several-fold extensibility of Fn fibrils involves the unfolding of type III modules. This could imply that Fn might play a significant role in mechanotransduction processes.

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Metadata

Authors
Smith, M. L., Gourdon, D., Little, W. C., Kubow, K. E., Eguiluz, R. A., Luna-Morris, S., & Vogel, V.
Venue
PLoS Biology
Publisher
Public Library of Science (PLoS)
Published
2007-10-02
Volume
5
Issue
10
Pages
e268
ISSN
  • 1544-9173 (ISSN-L)
  • 1545-7885
DOI
10.1371/journal.pbio.0050268
OpenAlex
W2163187600
Cited by
440
References
42
FWCI
8.43
Type
journal article
Language
en
Open access
gold

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