How Actin Polymerization and Myosin II-Mediated Tension Regulate Focal Adhesion Dynamics in Motile Cells

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Abstract

Focal adhesions (FAs) are multi-protein structures mediating interaction between cells and extracellular matrix. The formation and maturation of FAs depend on intracellular tension generated through the of actin filaments interacting with phosphorylated myosin II. Using live cell and confocal microscopy we evaluated the regulation of FA dynamics by actin polymerization and myosin II-mediated tension in motile cells. Our findings confirm that while partial inhibition of myosin II, through ROCK kinase or myosin II light chain kinase (MLCK) inhibitors, leads to the gradual shrinkage but increased stability of FAs, complete inhibition of myosin II phosphorylation results in disassembly of existing FAs followed by the formation of new small FAs at the cell edges. These FAs are rather stable, supported by cortical actin structures. Partial inhibition of actin polymerization with nanomolar doses of latrunculin B or cytochalasin D results in the similar effect, while complete inhibition leads to the rapid and irreversible disassembly of FAs and shrinkage of cell lamella. Overall, our results show that small FAs, which are normally short-living structures at the advancing cell edge, could be stabilized and persist, driven only by partial actin polymerization. These insights highlight the role of the interplay between actin and myosin in maintaining FA formation and dynamics.

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