Reversible stress softening of actin networks.
The mechanical properties of cells play an essential role in numerous physiological processes. Organized networks of semiflexible actin filaments determine cell stiffness and transmit force during mechanotransduction, cytokinesis, cell motility and other cellular shape changes. Although numerous actin-binding proteins have been identified that organize networks, the mechanical properties of actin networks with physiological architectures and concentrations have been difficult to measure quantitatively. Studies of mechanical properties in vitro have found that crosslinked networks of actin filaments formed in solution exhibit stress stiffening arising from the entropic elasticity of individual filaments or crosslinkers resisting extension. Here we report reversible stress-softening behaviour in actin networks reconstituted in vitro that suggests a critical role for filaments resisting compression. Using a modified atomic force microscope to probe dendritic actin networks (like those formed in the lamellipodia of motile cells), we observe stress stiffening followed by a regime of reversible stress softening at higher loads. This softening behaviour can be explained by elastic buckling of individual filaments under compression that avoids catastrophic fracture of the network. The observation of both stress stiffening and softening suggests a complex interplay between entropic and enthalpic elasticity in determining the mechanical properties of actin networks.
Chaudhuri
Ovijit
O
UC San Francisco /UC Berkeley Joint Graduate Group in Bioengineering and Department of Bioengineering, University of California at Berkeley, Berkeley, California 94720, USA.
Parekh
Sapun H
SH
Fletcher
Daniel A
DA
D000199:Actins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D003712:Dendrites / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D004548:Elasticity; D019277:Entropy; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D014783:Viscosity
D000199:Actins