Percolation mechanism drives actin gels to the critically connected state

Phys Rev E. 2016 May;93(5):052414. doi: 10.1103/PhysRevE.93.052414. Epub 2016 May 20.

Abstract

Cell motility and tissue morphogenesis depend crucially on the dynamic remodeling of actomyosin networks. An actomyosin network consists of an actin polymer network connected by cross-linker proteins and motor protein myosins that generate internal stresses on the network. A recent discovery shows that for a range of experimental parameters, actomyosin networks contract to clusters with a power-law size distribution [J. Alvarado, Nat. Phys. 9, 591 (2013)1745-247310.1038/nphys2715]. Here, we argue that actomyosin networks can exhibit a robust critical signature without fine-tuning because the dynamics of the system can be mapped onto a modified version of percolation with trapping (PT), which is known to show critical behavior belonging to the static percolation universality class without the need for fine-tuning of a control parameter. We further employ our PT model to generate experimentally testable predictions.

MeSH terms

  • Actin Cytoskeleton
  • Actins / chemistry*
  • Actomyosin / chemistry
  • Gels / chemistry*
  • Myosins / chemistry

Substances

  • Actins
  • Gels
  • Actomyosin
  • Myosins