Control of actin assembly and disassembly at filament ends

Curr Opin Cell Biol. 2000 Feb;12(1):97-103. doi: 10.1016/s0955-0674(99)00062-9.

Abstract

The most important discovery in the field is that the Arp2/3 complex nucleates assembly of actin filaments with free barbed ends. Arp2/3 also binds the sides of actin filaments to create a branched network. Arp2/3's nucleation activity is stimulated by WASP family proteins, some of which mediate signaling from small G-proteins. Listeria movement caused by actin polymerization can be reconstituted in vitro using purified proteins: Arp2/3 complex, capping protein, actin depolymerizing factor/cofilin, and actin. actin depolymerizing factor/cofilin increases the rate at which actin subunits leave pointed ends, and capping protein caps barbed ends.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actin Cytoskeleton / chemistry
  • Actin Cytoskeleton / metabolism*
  • Actin Depolymerizing Factors
  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins / metabolism*
  • Animals
  • CapZ Actin Capping Protein
  • Carrier Proteins / metabolism
  • Cell Movement
  • Cytoskeletal Proteins*
  • Gelsolin / metabolism
  • Humans
  • Microfilament Proteins / metabolism
  • Molecular Motor Proteins / metabolism
  • Muscle Proteins / metabolism
  • Tropomodulin

Substances

  • ACTR2 protein, human
  • ACTR3 protein, human
  • Actin Depolymerizing Factors
  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins
  • CapZ Actin Capping Protein
  • Carrier Proteins
  • Cytoskeletal Proteins
  • Gelsolin
  • Microfilament Proteins
  • Molecular Motor Proteins
  • Muscle Proteins
  • TMOD1 protein, human
  • Tropomodulin