Rate of treadmilling of actin filaments in vitro

J Mol Biol. 1986 Feb 20;187(4):627-31. doi: 10.1016/0022-2836(86)90341-4.

Abstract

Actin filaments capped at the barbed ends were formed by polymerizing monomeric actin onto a gelsolin-actin complex. The rate of depolymerization and polymerization of the pointed ends was determined by diluting gelsolin-capped actin filaments into various concentrations of monomeric actin. Under the conditions of the experiments (100 mM-KCl, 2 mM-MgCl2 at 37 degrees C) the rate constant of dissociation of subunits both from a shortening and a lengthening filament was found to be 0.21 s-1. As the rate of dissociation of subunits from the slow pointed end determines the rate of treadmilling, it is concluded that actin filaments treadmill with a rate of about 2 micron/h.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / analysis*
  • Actins*
  • Animals
  • Calcium-Binding Proteins
  • Cytoskeleton / analysis*
  • Gelsolin
  • Macromolecular Substances
  • Microfilament Proteins
  • Rabbits

Substances

  • Actins
  • Calcium-Binding Proteins
  • Gelsolin
  • Macromolecular Substances
  • Microfilament Proteins