Force transmission in migrating cells
Autor: | Maxime F. Fournier, Alexander B. Verkhovsky, Davide Carlo Ambrosi, Jean-Jacques Meister, Roger Sauser |
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Rok vydání: | 2010 |
Předmět: |
Keratinocytes
Cytochalasin D Traction (engineering) macromolecular substances Myosins Biology Heterocyclic Compounds 4 or More Rings Models Biological Traction force microscopy Article 03 medical and health sciences 0302 clinical medicine Cell Movement Tensile Strength Cell polarity Myosin Cell Adhesion Animals Cytoskeleton Cell Shape Research Articles Cells Cultured Actin 030304 developmental biology Protein Synthesis Inhibitors 0303 health sciences Fishes Cell Polarity Cell Biology Adhesion Actin cytoskeleton Biomechanical Phenomena Cell biology Actin Cytoskeleton Stress Mechanical 030217 neurology & neurosurgery |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
Popis: | Analysis of the relationship between actin network velocity and traction forces at the substrate shows that force transmission mechanisms vary with distinct regions of the cell. During cell migration, forces generated by the actin cytoskeleton are transmitted through adhesion complexes to the substrate. To investigate the mechanism of force generation and transmission, we analyzed the relationship between actin network velocity and traction forces at the substrate in a model system of persistently migrating fish epidermal keratocytes. Front and lateral sides of the cell exhibited much stronger coupling between actin motion and traction forces than the trailing cell body. Further analysis of the traction–velocity relationship suggested that the force transmission mechanisms were different in different cell regions: at the front, traction was generated by a gripping of the actin network to the substrate, whereas at the sides and back, it was produced by the network’s slipping over the substrate. Treatment with inhibitors of the actin–myosin system demonstrated that the cell body translocation could be powered by either of the two different processes, actomyosin contraction or actin assembly, with the former associated with significantly larger traction forces than the latter. |
Databáze: | OpenAIRE |
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