Multiscale polar theory of microtubule and motor-protein assemblies

Phys Rev Lett. 2015 Jan 30;114(4):048101. doi: 10.1103/PhysRevLett.114.048101. Epub 2015 Jan 27.

Abstract

Microtubules and motor proteins are building blocks of self-organized subcellular biological structures such as the mitotic spindle and the centrosomal microtubule array. These same ingredients can form new "bioactive" liquid-crystalline fluids that are intrinsically out of equilibrium and which display complex flows and defect dynamics. It is not yet well understood how microscopic activity, which involves polarity-dependent interactions between motor proteins and microtubules, yields such larger-scale dynamical structures. In our multiscale theory, Brownian dynamics simulations of polar microtubule ensembles driven by cross-linking motors allow us to study microscopic organization and stresses. Polarity sorting and cross-link relaxation emerge as two polar-specific sources of active destabilizing stress. On larger length scales, our continuum Doi-Onsager theory captures the hydrodynamic flows generated by polarity-dependent active stresses. The results connect local polar structure to flow structures and defect dynamics.

Publication types

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

MeSH terms

  • Liquid Crystals / chemistry
  • Microtubules / chemistry*
  • Microtubules / metabolism*
  • Models, Biological*
  • Models, Chemical*
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / metabolism*
  • Monte Carlo Method
  • Tensile Strength

Substances

  • Molecular Motor Proteins