Vimentin promotes collective cell migration through collagen networks via increased matrix remodeling and spheroid fluidity
14 affiliations
- 1BioInspired Institute, Syracuse University, Syracuse, NY, USA. [email protected]
- 2Physics Department, Syracuse University, Syracuse, NY, USA. [email protected]
- 3Syracuse University
- 4BioInspired Institute, Syracuse University, Syracuse, NY, USA
- 5Biomedical and Chemical Engineering Department, Syracuse University, Syracuse, NY, USA
- 6Physics Department, Syracuse University, Syracuse, NY, USA
- 7Upstate Medical University
- 8Department of Biological and Environmental Engineering, Cornell University, Ithaca, NY, USA
- 9Cornell University
- 10Department of Polymer Science and Engineering, Shanghai Jiao Tong University, Shanghai, China
- 11Shanghai Jiao Tong University
- 12Indian Creek Farm, Ithaca, NY, USA
- 13BioInspired Institute, Syracuse University, Syracuse, NY, USA. [email protected]
- 14Physics Department, Syracuse University, Syracuse, NY, USA. [email protected]
Abstract
Intermediate filaments (IF) are diverse and cell-type specific. The IF protein vimentin, expressed in mesenchymal cells and different cancer cells, is functionally associated with cell migration through fibrous tissues. Vimentin increases cell elongation needed for migration, yet also acts as a cytoskeletal cage that hinders cells squeezing through small spaces. To determine how vimentin facilitates cell migration through the extracellular matrix (ECM) and around neighboring cells in tissues, we examine the collective invasion of cell spheroids embedded in collagen networks. Unlike single-cell migration in collagen networks, the collective invasion of cells through the collagen network is increased by vimentin for both mouse embryonic fibroblasts (MEF) and co-cultures of MEF with MDA-MB-231 breast cancer cells. Using multiple experimental systems, we show that vimentin increases spheroid contractility and that vimentin-mediated collective cell expansion depends on matrix metalloproteinases (MMP), which degrade collagen networks. In addition, through advanced imaging and a computational 3D cell vertex model, we find that vimentin enhances the elongation of cells in spheroids embedded in collagen, indicating increased spheroid fluidity and active collagen contraction. Altogether, these results reveal new insights on vimentin's effects in enhancing collective cell migration in 3D matrix environments through collagen remodeling and tissue fluidity.
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BibTeX
@article{thanh2026vimentin,
title = {{Vimentin promotes collective cell migration through collagen networks via increased matrix remodeling and spheroid fluidity}},
author = {Minh Tri Ho Thanh and Arun Poudel and Shabeeb Ameen and Bobby Carroll and Mingming Wu and Pranav Soman and Tao Zhang and Jennifer M. Schwarz and Alison E. Patteson},
journal = {Communications Biology},
year = {2026},
month = jun,
doi = {10.1038/s42003-026-10506-3},
url = {https://doi.org/10.1038/s42003-026-10506-3},
note = {CC BY},
}
RIS
TY - JOUR
TI - Vimentin promotes collective cell migration through collagen networks via increased matrix remodeling and spheroid fluidity
AU - Minh Tri Ho Thanh
AU - Arun Poudel
AU - Shabeeb Ameen
AU - Bobby Carroll
AU - Mingming Wu
AU - Pranav Soman
AU - Tao Zhang
AU - Jennifer M. Schwarz
AU - Alison E. Patteson
PY - 2026
DA - 2026/06/18
JO - Communications Biology
DO - 10.1038/s42003-026-10506-3
UR - https://doi.org/10.1038/s42003-026-10506-3
AB - Intermediate filaments (IF) are diverse and cell-type specific. The IF protein vimentin, expressed in mesenchymal cells and different cancer cells, is functionally associated with cell migration through fibrous tissues. Vimentin increases cell elongation needed for migration, yet also acts as a cytoskeletal cage that hinders cells squeezing through small spaces. To determine how vimentin facilitates cell migration through the extracellular matrix (ECM) and around neighboring cells in tissues, we examine the collective invasion of cell spheroids embedded in collagen networks. Unlike single-cell migration in collagen networks, the collective invasion of cells through the collagen network is increased by vimentin for both mouse embryonic fibroblasts (MEF) and co-cultures of MEF with MDA-MB-231 breast cancer cells. Using multiple experimental systems, we show that vimentin increases spheroid contractility and that vimentin-mediated collective cell expansion depends on matrix metalloproteinases (MMP), which degrade collagen networks. In addition, through advanced imaging and a computational 3D cell vertex model, we find that vimentin enhances the elongation of cells in spheroids embedded in collagen, indicating increased spheroid fluidity and active collagen contraction. Altogether, these results reveal new insights on vimentin's effects in enhancing collective cell migration in 3D matrix environments through collagen remodeling and tissue fluidity.
SN - 2399-3642
ER -