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Publication Detail
Arp2/3 complex-mediated actin polymerisation occurs on specific pre-existing networks in cells and requires spatial restriction to sustain functional lamellipod extension
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Shao D, Forge A, Munro PMG, and Bailly M
  • Publication date:
  • Pagination:
    395, 414
  • Journal:
    Cell Motility and the Cytoskeleton
  • Volume:
  • Issue:
  • Print ISSN:
  • Keywords:
    Actin-Related Protein 2-3 Complex/genetics/isolation & purification/*metabolism Actins/*metabolism Animals Blood Platelets/chemistry Cell Line, Tumor Cytoskeleton/*drug effects/ultrastructure Epidermal Growth Factor/pharmacology Epithelial Cells/drug effe
  • Addresses:
    Division of Cell Biology, UCL Institute of Ophthalmology, London, United Kingdom
  • Notes:
    JulArp2/3 complex-mediated actin polymerisation occurs on specific pre-existing networks in cells and requires spatial restriction to sustain functional lamellipod extension16619224Wellcome Trust Journal Article Research Support, Non-U.S. Gov\'t United Stateseng
The classical Arp2/3-mediated dendritic network defines the cytoskeleton at the leading edge of crawling cells, and it is generally assumed that Arp2/3-mediated actin polymerization generates the force necessary to extend lamellipods. Our previous work suggested that successful lamellipod extension required not only free barbed ends for actin polymerization but also a proper ultrastructural organization of the cytoskeleton. To further explore the structural role of the Arp2/3 complex-mediated networks in lamellipod morphology and function, we performed a detailed analysis of the ultrastructure of the Arp2/3-mediated networks, using the WA domains of Scar and WASp to generate mislocalised Arp2/3 networks in vivo, and to reconstruct de novo Arp2/3-mediated actin nucleation and polymerization on extracted cytoskeletons. We present here evidence that spatially unrestricted Arp2/3-mediated networks are intrinsically three-dimensional and multilayered by nature and, as such, cannot sustain significant polarized extension. Furthermore, such networks polymerize only at preferred locations in extracted cells, corresponding to pre-existing Arp2/3 networks, suggesting that the specific molecular organization of the actin cytoskeleton, in terms of structure and/or biochemical composition, dictates the location of Arp2/3 complex-mediated actin polymerization. We propose that successful lamellipod extension depends not only on localized actin polymerization mediated through local signalling, but also on spatial restriction of the Arp2/3 complex-mediated nucleation of actin polymerization, both in terms of location within the cell and ultrastructural organization of the resulting network
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