Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix

Verfasser / Beitragende:
[Kristopher E. Kubow, Radmila Vukmirovic, Zhe Lin, Enrico; id_orcid 0000-0002-7577-9042 Klotzsch, Michael L. Smith, Delphine Gourdon, Sheila Luna, Viola Vogel]
Ort, Verlag, Jahr:
2015
Enthalten in:
Nature Communications, 6, p. 8026
Format:
Artikel (online)
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024 7 0 |a 10.3929/ethz-b-000103188  |2 doi 
024 7 0 |a 10.1038/ncomms9026  |2 doi 
035 |a (ETHRESEARCH)oai:www.research-collecti.ethz.ch:20.500.11850/103188 
245 0 0 |a Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix  |h [Elektronische Daten]  |c [Kristopher E. Kubow, Radmila Vukmirovic, Zhe Lin, Enrico; id_orcid 0000-0002-7577-9042 Klotzsch, Michael L. Smith, Delphine Gourdon, Sheila Luna, Viola Vogel] 
246 0 |a Nat Commun 
506 |a Open access  |2 ethresearch 
520 3 |a Despite the crucial role of extracellular matrix (ECM) in directing cell fate in healthy and diseased tissues—particularly in development, wound healing, tissue regeneration and cancer—the mechanisms that direct the assembly and regulate hierarchical architectures of ECM are poorly understood. Collagen I matrix assembly in vivo requires active fibronectin (Fn) fibrillogenesis by cells. Here we exploit Fn-FRET probes as mechanical strain sensors and demonstrate that collagen I fibres preferentially co-localize with more-relaxed Fn fibrils in the ECM of fibroblasts in cell culture. Fibre stretch-assay studies reveal that collagen I's Fn-binding domain is responsible for the mechano-regulated interaction. Furthermore, we show that Fn-collagen interactions are reciprocal: relaxed Fn fibrils act as multivalent templates for collagen assembly, but once assembled, collagen fibres shield Fn fibres from being stretched by cellular traction forces. Thus, in addition to the well-recognized, force-regulated, cell-matrix interactions, forces also tune the interactions between different structural ECM components. 
540 |a Creative Commons Attribution 4.0 International  |u http://creativecommons.org/licenses/by/4.0  |2 ethresearch 
700 1 |a Kubow  |D Kristopher E.  |e joint author 
700 1 |a Vukmirovic  |D Radmila  |e joint author 
700 1 |a Lin  |D Zhe  |e joint author 
700 1 |a Klotzsch  |D Enrico; id_orcid 0000-0002-7577-9042  |e joint author 
700 1 |a Smith  |D Michael L.  |e joint author 
700 1 |a Gourdon  |D Delphine  |e joint author 
700 1 |a Luna  |D Sheila  |e joint author 
700 1 |a Vogel  |D Viola  |e joint author 
773 0 |t Nature Communications  |d London : Nature Publishing Group  |g 6, p. 8026  |x 2041-1723 
856 4 0 |u http://hdl.handle.net/20.500.11850/103188  |q text/html  |z WWW-Backlink auf das Repository (Open access) 
908 |D 1  |a Journal Article  |2 ethresearch 
950 |B ETHRESEARCH  |P 856  |E 40  |u http://hdl.handle.net/20.500.11850/103188  |q text/html  |z WWW-Backlink auf das Repository (Open access) 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Kubow  |D Kristopher E.  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Vukmirovic  |D Radmila  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Lin  |D Zhe  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Klotzsch  |D Enrico; id_orcid 0000-0002-7577-9042  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Smith  |D Michael L.  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Gourdon  |D Delphine  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Luna  |D Sheila  |e joint author 
950 |B ETHRESEARCH  |P 700  |E 1-  |a Vogel  |D Viola  |e joint author 
950 |B ETHRESEARCH  |P 773  |E 0-  |t Nature Communications  |d London : Nature Publishing Group  |g 6, p. 8026  |x 2041-1723 
898 |a BK010053  |b XK010053  |c XK010000 
949 |B ETHRESEARCH  |F ETHRESEARCH  |b ETHRESEARCH  |j Journal Article  |c Open access