Document Type

Journal Article

Publication Date

3-15-2014

Journal

Molecular Biology of the Cell

Volume

Volume 25, Issue 6

Inclusive Pages

776-790

DOI

10.1091/mbc.E12-12-0900

Keywords

Epithelial Cells--metabolism; Lens, Crystalline--metabolism; Vimentin--genetics; Wound Healing--genetics

Abstract

Mock cataract surgery provides a unique ex vivo model for studying wound repair in a clinically relevant setting. Here wound healing involves a classical collective migration of the lens epithelium, directed at the leading edge by an innate mesenchymal subpopulation of vimentin-rich repair cells. We report that vimentin is essential to the function of repair cells as the directors of the wound-healing process. Vimentin and not actin filaments are the predominant cytoskeletal elements in the lamellipodial extensions of the repair cells at the wound edge. These vimentin filaments link to paxillin-containing focal adhesions at the lamellipodial tips. Microtubules are involved in the extension of vimentin filaments in repair cells, the elaboration of vimentin-rich protrusions, and wound closure. The requirement for vimentin in repair cell function is revealed by both small interfering RNA vimentin knockdown and exposure to the vimentin-targeted drug withaferin A. Perturbation of vimentin impairs repair cell function and wound closure. Coimmunoprecipitation analysis reveals for the first time that myosin IIB is associated with vimentin, linking vimentin function in cell migration to myosin II motor proteins. These studies reveal a critical role for vimentin in repair cell function in regulating the collective movement of the epithelium in response to wounding.

Comments

This research was originally published in Molecular Biology of the Cell, 25(6), 776-790, DOI:10.1091/mbc.E12-12-0900. Copyright © 2014 The American Society for Cell Biology.

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 License.

Peer Reviewed

1

Open Access

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