Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins

Laurent Blanchoin, Kurt J. Amann, Henry N. Higgs, Jean-Baptiste Marchand, Donald A. Kaiser and Thomas D. Pollard ()
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Laurent Blanchoin: Structural Biology Laboratory, Salk Institute for Biological Studies
Kurt J. Amann: Structural Biology Laboratory, Salk Institute for Biological Studies
Henry N. Higgs: Structural Biology Laboratory, Salk Institute for Biological Studies
Jean-Baptiste Marchand: Structural Biology Laboratory, Salk Institute for Biological Studies
Donald A. Kaiser: Structural Biology Laboratory, Salk Institute for Biological Studies
Thomas D. Pollard: Structural Biology Laboratory, Salk Institute for Biological Studies

Nature, 2000, vol. 404, issue 6781, 1007-1011

Abstract: Abstract Most nucleated cells crawl about by extending a pseudopod that is driven by the polymerization of actin filaments in the cytoplasm behind the leading edge of the plasma membrane1,2. These actin filaments are linked into a network by Y-branches, with the pointed end of each filament attached to the side of another filament and the rapidly growing barbed end facing forward3. Because Arp2/3 complex nucleates actin polymerization and links the pointed end to the side of another filament in vitro, a dendritic nucleation model has been proposed4 in which Arp2/3 complex initiates filaments from the sides of older filaments. Here we report, by using a light microscopy assay, many new features of the mechanism. Branching occurs during, rather than after, nucleation by Arp2/3 complex activated by the Wiskott–Aldrich syndrome protein (WASP) or Scar protein; capping protein and profilin act synergistically with Arp2/3 complex to favour branched nucleation; phosphate release from aged actin filaments favours dissociation of Arp2/3 complex from the pointed ends of filaments; and branches created by Arp2/3 complex are relatively rigid. These properties result in the automatic assembly of the branched actin network after activation by proteins of the WASP/Scar family and favour the selective disassembly of proximal regions of the network.

Date: 2000
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DOI: 10.1038/35010008

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