Self-organization and Mechanical Properties of Active Filament Bundles

A phenomenological description for active bundles of polar filaments is presented. The activity of the bundle results from crosslinks, that induce relative displacements between the aligned filaments. Our generic description is based on momentum conservation within the bundle. By specifying the internal forces, a simple minimal model for the bundle dynamics is obtained, capturing generic dynamic behaviors. In particular, contracted states as well as solitary and oscillatory waves appear through dynamic instabilities. The introduction of filament adhesion leads to self-organized persistent filament transport. Furthermore, calculating the tension, homogeneous bundles are shown to be able to actively contract and to perform work against external forces. Our description is motivated by dynamic phenomena in the cytoskeleton and could apply to stress-fibers and self-organization phenomena during cell-locomotion.Comment: 19 pages, 10 figure

Gradient of rigidity in the lamellipodia of migrating cells revealed by atomic force microscopy.

Changes in mechanical properties of the cytoplasm have been implicated in cell motility, but there is little information about these properties in specific regions of the cell at specific stages of the cell migration process. Fish epidermal keratocytes with their stable shape and steady motion represent an ideal system to elucidate temporal and spatial dynamics of the mechanical state of the cytoplasm. As the shape of the cell does not change during motion and actin network in the lamellipodia is nearly stationary with respect to the substrate, the spatial changes in the direction from the front to the rear of the cell reflect temporal changes in the actin network after its assembly at the leading edge. We have utilized atomic force microscopy to determine the rigidity of fish keratocyte lamellipodia as a function of time/distance from the leading edge. Although vertical thickness remained nearly constant throughout the lamellipodia, the rigidity exhibited a gradual but significant decrease from the front to the rear of the lamellipodia. The rigidity profile resembled closely the actin density profile, suggesting that the dynamics of rigidity are due to actin depolymerization. The decrease of rigidity may play a role in facilitating the contraction of the actin-myosin network at the lamellipodium/cell body transition zone