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The Role Of Vimentin–Nuclear Interactions In Persistent Cell Motility Through Confined Spaces, Sarthak Gupta, Alison E. Patteson, J. M. Schwarz
The Role Of Vimentin–Nuclear Interactions In Persistent Cell Motility Through Confined Spaces, Sarthak Gupta, Alison E. Patteson, J. M. Schwarz
Physics - All Scholarship
The ability of cells to move through small spaces depends on the mechanical properties of the cellular cytoskeleton and on nuclear deformability. In mammalian cells, the cytoskeleton is composed of three interacting, semi-flexible polymer networks: actin, microtubules, and intermediate filaments (IF). Recent experiments of mouse embryonic fibroblasts with and without vimentin have shown that the IF vimentin plays a role in confined cell motility. Here, we develop a minimal model of a cell moving through a microchannel that incorporates explicit effects of actin and vimentin and implicit effects of microtubules. Specifically, the model consists of a cell with an actomyosin …
Vimentin Tunes Cell Migration On Collagen By Controlling Β1 Integrin Activation And Clustering, Zofia Ostrowska-Podhorodecka, Isabel Ding, Wilson Lee, Jelena Tanic, Sevil Abbasi, Pamma D. Arora, Richard S. Liu, Alison E. Patteson, Paul A. Janmey, Christopher A. Mcculloch
Vimentin Tunes Cell Migration On Collagen By Controlling Β1 Integrin Activation And Clustering, Zofia Ostrowska-Podhorodecka, Isabel Ding, Wilson Lee, Jelena Tanic, Sevil Abbasi, Pamma D. Arora, Richard S. Liu, Alison E. Patteson, Paul A. Janmey, Christopher A. Mcculloch
Physics - All Scholarship
Vimentin is a structural protein that is required for mesenchymal cell migration and directly interacts with actin, β1 integrin and paxillin. We examined how these interactions enable vimentin to regulate cell migration on collagen. In fibroblasts, depletion of vimentin increased talin-dependent activation of β1 integrin by more than 2-fold. Loss of vimentin was associated with reduction of β1 integrin clustering by 50% and inhibition of paxillin recruitment to focal adhesions by more than 60%, which was restored by vimentin expression. This reduction of paxillin was associated with 65% lower Cdc42 activation, a 60% reduction of cell extension formation and a …