Physics Commons^™

Extracellular Vimentin Is Sufficient To Promote Cell Attachment, Spreading, And Motility By A Mechanism Involving N-Acetyl Glucosamine-Containing Structures, Robert Bucki, Daniel V. Iwamoto, Xuechen Shi, Katherine E. Kerr, Fitzroy J. Byfield, Lukasz Suprewicz, Karol Sklodowski, Julian Sutaria, Pawel Misiak, Agnieszka Z. Wilczewska, Sekar Ramachandran, Aaron Wolfe, Minh H. Thanh, Eli Whalen, Alison E. Patteson, Paul A. Janmey

Physics - All Scholarship

Vimentin intermediate !laments form part of the cytoskeleton

of mesenchymal cells, but under pathological conditions often

associatedwith in"ammation, vimentin !laments depolymerize as

the result of phosphorylation or citrullination, and vimentin

oligomers are secreted or released into the extracellular environment.

In the extracellular space, vimentin can bind surfaces of cells

and the extracellular matrix, and the interaction between extracellular

vimentin and cells can trigger changes in cellular functions,

such as activation of !broblasts to a !brotic phenotype. The

mechanism by which extracellular vimentin binds external cell

membranes and whether vimentin alone can act as an adhesive

anchor for cells is largely …

Unique Role Of Vimentin Networks In Compression Stiffening Of Cells And Protection Of Nuclei From Compressive Stress, Katarzyna Pogoda, Fitzroy Byfield, Piotr Deptuła, Mateusz Cieśluk, Łukasz Suprewicz, Karol Skłodowski, Jordan L. Shivers, Anne Van Oosten, Katrina Cruz, Ekaterina Tarasovetc, Ekaterina L. Grishchuk, Fred C. Mackintosh, Robert Bucki, Alison E. Patteson, Paul A. Janmey

Physics - All Scholarship

In this work, we investigate whether stiffening in compression is a feature of single cells and whether the intracellular polymer networks that comprise the cytoskeleton (all of which stiffen with increasing shear strain) stiffen or soften when subjected to compressive strains. We find that individual cells, such as fibroblasts, stiffen at physiologically relevant compressive strains, but genetic ablation of vimentin diminishes this effect. Further, we show that unlike networks of purified F-actin or microtubules, which soften in compression, vimentin intermediate filament networks stiffen in both compression and extension, and we present a theoretical model to explain this response based on …

Vimentin Intermediate Filaments Mediate Cell Morphology On Viscoelastic Substrates, Maxx Swoger, Sarthak Gupta, Elisabeth E. Charrier, Michael Bates, Heidi Hehnly, Alison E. Patteson

Physics - All Scholarship

The ability of cells to take and change shape is a fundamental feature underlying development, wound repair, and tissue maintenance. Central to this process is physical and signaling interactions between the three cytoskeletal polymeric networks: F-actin, microtubules, and intermediate filaments (IFs). Vimentin is an IF protein that is essential to the mechanical resilience of cells and regulates cross-talk among the cytoskeleton, but its role in how cells sense and respond to the surrounding extracellular matrix is largely unclear. To investigate vimentin’s role in substrate sensing, we designed polyacrylamide hydrogels that mimic the elastic and viscoelastic nature of in vivo tissues. …

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

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 …

The Vimentin Cytoskeleton: When Polymer Physics Meets Cell Biology, Alison E. Patteson, Robert J. Carroll, Daniel V. Iwamoto, Paul A. Janmey

Physics - All Scholarship

The proper functions of tissues depend on the ability of cells to withstand stress and maintain shape. Central to this process is the cytoskeleton, comprised of three polymeric networks: F-actin, microtubules, and intermediate filaments (IFs). IF proteins are among the most abundant cytoskeletal proteins in cells; yet they remain some of the least understood. Their structure and function deviate from those of their cytoskeletal partners, F-actin and microtubules. IF networks show a unique combination of extensibility, flexibility and toughness that confers mechanical resilience to the cell. Vimentin is an IF protein expressed in mesenchymal cells. This review highlights exciting new …