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Cell adhesion

Collagen fibril self-assembly

Nature Cell Biology volume 25, page 1240 (2023)Cite this article

Collagen is an abundant extracellular matrix protein. However, how precisely collagen protofilaments are assembled into ordered fibrils in vivo remains unclear. Using modelling and in vivo experimental data, Revell et al. suggest that protomeric collagen is secreted then progressively assembled extracellularly into fibrils in the mouse embryonic tail.

The authors used a two-dimensional phase-field crystal model, which accounts for crystal self-assembly, to suggest that collagen fibrils form over time and that protomeric collagen is present in extracellular spaces before fibril formation. Through electron microscopy of embryonic mouse tails, Revell et al. found fibrils at embryonic day 13.5 (E13.5). They then utilized laser-capture microdissection coupled with mass spectrometry to analyse specific tail regions over time and found that collagen protomers increase and peak at E13.5, before steadily decreasing. This is in spite of collagen biosynthetic proteins that peak at later stages. These results suggest an initial increase in extracellular collagen protomers that are progressively incorporated into fibrils.

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  1. Nature Cell Biology https://www.nature.com/ncb/

    Daryl J. V. David

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  1. Daryl J. V. David
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Correspondence to Daryl J. V. David.

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David, D.J.V. Collagen fibril self-assembly. Nat Cell Biol 25, 1240 (2023). https://doi.org/10.1038/s41556-023-01236-3

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