Regulation of actin filament assembly by Arp2/3 complex and formins

Annu Rev Biophys Biomol Struct. 2007;36:451-77. doi: 10.1146/annurev.biophys.35.040405.101936.


This review summarizes what is known about the biochemical and biophysical mechanisms that initiate the assembly of actin filaments in cells. Assembly and disassembly of these filaments contribute to many types of cellular movements. Numerous proteins regulate actin assembly, but Arp2/3 complex and formins are the focus of this review because more is known about them than other proteins that stimulate the formation of new filaments. Arp2/3 complex is active at the leading edge of motile cells, where it produces branches on the sides of existing filaments. Growth of these filaments produces force to protrude the membrane. Crystal structures, reconstructions from electron micrographs, and biophysical experiments have started to map out the steps through which proteins called nucleation-promoting factors stimulate the formation of branches. Formins nucleate and support the elongation of unbranched actin filaments for cytokinesis and various types of actin filament bundles. Formins associate processively with the fast-growing ends of filaments and protect them from capping.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Actin-Related Protein 2-3 Complex / chemistry*
  • Actins / chemistry*
  • Adenosine Triphosphate / chemistry
  • Animals
  • Biophysics / methods
  • Cortactin / chemistry*
  • Crystallization
  • Humans
  • Hydrolysis
  • Kinetics
  • Models, Biological
  • Molecular Conformation
  • Profilins / chemistry*
  • Protein Conformation
  • Thermodynamics


  • Actin-Related Protein 2-3 Complex
  • Actins
  • Cortactin
  • Profilins
  • Adenosine Triphosphate