Actin filament length tunes elasticity of flexibly cross-linked actin networks.
Networks of the cytoskeletal biopolymer actin cross-linked by the compliant protein filamin form soft gels that stiffen dramatically under shear stress. We demonstrate that the elasticity of these networks shows a strong dependence on the mean length of the actin polymers, unlike networks with small, rigid cross-links. This behavior is in agreement with a model of rigid filaments connected by multiple flexible linkers.
Kasza
K E
KE
School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts, USA.
Broedersz
C P
CP
Koenderink
G H
GH
Lin
Y C
YC
Messner
W
W
Millman
E A
EA
Nakamura
F
F
Stossel
T P
TP
Mackintosh
F C
FC
Weitz
D A
DA
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D003285:Contractile Proteins / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D055119:Elastic Modulus / Q000187:drug effects; D004548:Elasticity / Q000187:drug effects / Q000502:physiology*; D064448:Filamins; D018260:Gelsolin / Q000378:metabolism; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism; D017711:Nonlinear Dynamics; D018583:Pliability / Q000187:drug effects; D011817:Rabbits; D013312:Stress, Physiological / Q000187:drug effects; D014783:Viscosity / Q000187:drug effects
D000199:Actins; D003285:Contractile Proteins; D003432:Cross-Linking Reagents; D064448:Filamins; D018260:Gelsolin; D008840:Microfilament Proteins