Actin filament length tunes elasticity of flexibly cross-linked actin networks

Biophys J. 2010 Aug 9;99(4):1091-100. doi: 10.1016/j.bpj.2010.06.025.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actin Cytoskeleton / ultrastructure
  • Actins / metabolism*
  • Actins / ultrastructure
  • Animals
  • Contractile Proteins / metabolism
  • Cross-Linking Reagents / pharmacology*
  • Elastic Modulus / drug effects
  • Elasticity / drug effects
  • Elasticity / physiology*
  • Filamins
  • Gelsolin / metabolism
  • Humans
  • Microfilament Proteins / metabolism
  • Nonlinear Dynamics
  • Pliability / drug effects
  • Rabbits
  • Stress, Physiological / drug effects
  • Viscosity / drug effects

Substances

  • Actins
  • Contractile Proteins
  • Cross-Linking Reagents
  • Filamins
  • Gelsolin
  • Microfilament Proteins