A new mechanism of fibronectin fibril assembly revealed by live imaging and super-resolution microscopy

Document Type

Article

Publication Date

8-1-2022

Abstract

Fibronectin (Fn1) fibrils have long been viewed as continuous fibers composed of extended, periodically aligned Fn1 molecules. However, our live-imaging and single-molecule localization microscopy data are inconsistent with this traditional view and show that Fn1 fibrils are composed of roughly spherical nanodomains containing six to eleven Fn1 dimers. As they move toward the cell center, Fn1 nanodomains become organized into linear arrays, in which nanodomains are spaced with an average periodicity of 105±17 nm. Periodical Fn1 nanodomain arrays can be visualized between cells in culture and within tissues; they are resistant to deoxycholate treatment and retain nanodomain periodicity in the absence of cells. The nanodomain periodicity in fibrils remained constant when probed with antibodies recognizing distinct Fn1 epitopes or combinations of antibodies recognizing epitopes spanning the length of Fn1. Treatment with FUD, a peptide that binds the Fn1 N-terminus and disrupts Fn1 fibrillogenesis, blocked the organization of Fn1 nanodomains into periodical arrays. These studies establish a new paradigm of Fn1 fibrillogenesis.

Identifier

85137127435 (Scopus)

Publication Title

Journal of Cell Science

External Full Text Location

https://doi.org/10.1242/jcs.260120

e-ISSN

14779137

ISSN

00219533

PubMed ID

35851804

Issue

16

Volume

135

Grant

836254

Fund Ref

National Institutes of Health

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