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Vimentin regulates the assembly and function of matrix adhesions
Author(s) -
OstrowskaPodhorodecka Zofia,
McCulloch Christopher A.
Publication year - 2021
Publication title -
wound repair and regeneration
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.847
H-Index - 109
eISSN - 1524-475X
pISSN - 1067-1927
DOI - 10.1111/wrr.12920
Subject(s) - vimentin , myofibroblast , focal adhesion , microbiology and biotechnology , extracellular matrix , fibroblast , intermediate filament protein , mesenchymal stem cell , intermediate filament , cell adhesion , cell migration , matrix (chemical analysis) , integrin , context (archaeology) , cell , chemistry , biology , cytoskeleton , immunology , pathology , signal transduction , cell culture , medicine , genetics , biochemistry , immunohistochemistry , fibrosis , paleontology , chromatography
The intermediate filament protein vimentin is a widely used phenotypic marker for identifying cells of the mesenchymal linkage such as fibroblasts and myofibroblasts, but the full repertoire of vimentin's functional attributes has not been fully explored. Here we consider how vimentin, in addition to its contributions to mechanical stabilization of cell structure, also helps to control the assembly of cell adhesions and migration through collagen matrices. While the assembly and function of matrix adhesions are critical for the differentiation of myofibroblasts and many other types of adherent cells, a potential mechanism that explains how vimentin affects the recruitment and abundance of centrally important proteins in cell adhesions has been elusive. Here we review recent data indicating that vimentin plays a central regulatory role in the assembly of focal adhesions which form in response to the attachment to collagen. We show that in particular, vimentin is a key organizer of the β1 integrin adhesive machinery, which affects cell migration through collagen. This review provides a comprehensive picture of the surprisingly broad array of processes and molecules with which vimentin interacts to affect cell function in the context of fibroblast and myofibroblast adhesion and migration on collagen.