Most cells migrate under the appropriate conditions or stimuli; understanding the mechanisms of migration, the players involved, and their regulation, is pivotal to tackle the pathological situations … Expand. Mismatch in mechanical and adhesive properties induces pulsating cancer cell migration in epithelial monolayer.
View 2 excerpts, cites background. Collective cell migration in development. Collective cell migration is a key process during the development of most organisms. It can involve either the migration of closely packed mesenchymal cells that make dynamic contacts with frequently … Expand. Cell movement is guided by the rigidity of the substrate.
Prespecification and plasticity: shifting mechanisms of cell migration. Migration of zebrafish primordial germ cells: a role for myosin contraction and cytoplasmic flow. Proteolytic interstitial cell migration: a five-step process. Directional control of cell motility through focal adhesion positioning and spatial control of Rac activation. Chemokine signaling mediates self-organizing tissue migration in the zebrafish lateral line. Mechanics, malignancy, and metastasis: The force journey of a tumor cell.
Related Papers. Filaments within cells like Amoeba run the length of the cell and carry vesicles of material to the leading edge. In a burst of activity the front of the cell fuses with these microfilament containing vesicles and cause an outward movement and a thrusting forward. The membrane attaches to the surface beneath and back at the trailing edge the membrane is released from the surface.
Here, vesicles are pinched off, pulling the membrane inwards and pulling the cell forwards. The net effect is to move the whole cell in the required direction. More rapid movements can be accomplished by using specialized organelles which extend from the surface of a cell. Cilia are short projections from the cell surface that are filled along their length with microtubules.
Stress fiber-like structures connected to FAs are required for stretch-induced vinculin accumulation at FAs. In work recently published by Dr Hiroaki Hirata, a postdoctoral fellow in the laboratory of Prof Chwee Teck Lim of the Mechanobiology Institute, National University of Singapore, and Prof Masahiro Sokabe of the Nagoya University Graduate School of Medicine in Japan, a key element in the machinery that drives cell movement was described for the first time in living cells.
It is well established that individual cells possess distinct structures, known as focal adhesions, which allow them to grip onto a surface and generate force internally. Inside the cell, focal adhesions are physically linked to a network of filaments or cables, composed of a protein called actin, that form near the cell membrane. These are highly dynamic and are constantly undergoing assembly and disassembly.
Due to their dynamic nature, as well as the activity of a protein known as myosin, the actin filaments are constantly moving inwards, towards the center of the cell. Force-dependent binding of vinculin to talin has been reported in in vitro and in silico studies.
We have, for the first time demonstrated that this force- dependent binding indeed occurs at focal adhesions in living cells.
The question that scientists have long sought to understand is how a moving actin filament network can be physically linked to a fixed adhesion site, and how this linkage generates cell movement.
It was akin to playing tug-of-war with a lubricated rope. However, the actin binding protein talin was also known to possess multiple vinculin binding sites and the force-dependent binding of vinculin to talin had been observed in both in vitro and in silico studies. It had just never been observed in living cells. Hirata et al have now shown that indeed, vinculin binding to talin does occur in living cells.
Although talin will slip beyond 2pN, this encourages the accumulation of vinculin at the focal adhesion site, and, before the link slips, multiple vinculin proteins bind to the complex, forming an integrin- talin-vinculin-actin link.
Each vinculin molecule was shown to withstand 2. With multiple vinculin proteins able to bind to this complex, a far greater force was sustained, and this is sufficient to tether the actin filament network to focal adhesions.
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