Attachment conditions control actin filament buckling and the production of forces

Biophys J. 2007 Apr 1;92(7):2546-58. doi: 10.1529/biophysj.106.094672. Epub 2007 Jan 5.

Abstract

Actin polymerization is the driving force for a large number of cellular processes. Formation of lamellipodia and filopodia at the leading edge of motile cells requires actin polymerization induced mechanical deformation of the plasma membrane. To generate different types of membrane protrusions, the mechanical properties of actin filaments can be constrained by interacting proteins. A striking example of such constraint is the buckling of actin filaments generated in vitro by the cooperative effect of a processive actin nucleating factor (formin) and a molecular motor (myosin II). We developed a physical model based on equations for an elastic rod that accounts for actin filament buckling. Both ends of the rod were maintained in a fixed position in space and we considered three sets of boundary conditions. The model qualitatively and quantitatively reproduces the shape distribution of actin filaments. We found that actin polymerization counterpoises a force in the range 0.4-1.6 pN for moderate end-to-end distance (approximately 1 microm) and could be as large as 10 pN for shorter distances. If the actin rod attachment includes a spring, we discovered that the stiffness must be in the range 0.1-1.2 pN/nm to account for the observed buckling.

MeSH terms

  • Actin Cytoskeleton / chemistry*
  • Actin Cytoskeleton / ultrastructure*
  • Adhesiveness
  • Computer Simulation
  • Microscopy, Fluorescence / methods*
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / ultrastructure*
  • Motion
  • Protein Conformation
  • Stress, Mechanical

Substances

  • Molecular Motor Proteins