How Force Affects Fibronectin in Living Cells
Author Information
Author(s): Smith Michael L, Gourdon Delphine, Little William C, Kubow Kristopher E, Eguiluz R. Andresen, Luna-Morris Sheila, Vogel Viola
Primary Institution: Swiss Federal Institute of Technology Zurich
Hypothesis
Whether mechanically unfolded fibronectin (Fn) is present within native extracellular matrix fibrils is controversial.
Conclusion
The study concludes that the resting state of Fn fibrils does not contain Fn molecules with crossed-over arms, and that the extensibility of Fn fibrils involves the unfolding of type III modules.
Supporting Evidence
- 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 was never detected within extracellular matrix fibrils.
Takeaway
Fibronectin, a protein in our body, can stretch and change shape when cells pull on it, which might help cells communicate and respond to their environment.
Methodology
Fluorescence resonance energy transfer (FRET) was used to study the conformational changes of fibronectin in living cells.
Limitations
The study may not account for all possible conformations of fibronectin in different cellular contexts.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website