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Publication Detail
Clathrin is required for Scar/Wave-mediated lamellipodium formation
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Article
  • Authors:
    Gautier JJ, Lomakina ME, Bouslama-Oueghlani L, Derivery E, Beilinson H, Faigle W, Loew D, Louvard D, Echard A, Alexandrova AY, Baum B, Gautreau A
  • Publisher:
    COMPANY OF BIOLOGISTS LTD
  • Publication date:
    15/10/2011
  • Pagination:
    3414, 3427
  • Journal:
    J CELL SCI
  • Volume:
    124
  • Issue:
    20
  • Print ISSN:
    0021-9533
  • Language:
    EN
  • Keywords:
    Scar/Wave complex, Arp2/3 complex, Actin, Clathrin, Lamellipodium, ACTIN POLYMERIZATION, ARP2/3 COMPLEX, CELL-MIGRATION, WAVE COMPLEX, MEMBRANE TENSION, LEADING-EDGE, PROTEIN, RAC, WASP, CYTOSKELETON
  • Addresses:
    Gautreau, A
    CNRS
    UPR3082
    Lab Enzymol & Biochim Struct
    F-91198
    Gif Sur Yvette
    France

    CNRS
    UMR144
    F-75248
    Paris
    05
    France

    CNRS
    URA 2582
    F-75724
    Paris
    15
    France

    UCL
    Dept Cell & Dev Biol
    London
    WC1E 6BT
    England
Abstract
The Scar/Wave complex (SWC) generates lamellipodia through Arp2/3-dependent polymerisation of branched actin networks. In order to identify new SWC regulators, we conducted a screen in Drosophila cells combining proteomics with functional genomics. This screen identified Clathrin heavy chain (CHC) as a protein that binds to the SWC and whose depletion affects lamellipodium formation. This role of CHC in lamellipodium formation can be uncoupled from its role in membrane trafficking by several experimental approaches. Furthermore, CHC is detected in lamellipodia in the absence of the adaptor and accessory proteins of endocytosis. We found that CHC overexpression decreased membrane recruitment of the SWC, resulting in reduced velocity of protrusions and reduced cell migration. By contrast, when CHC was targeted to the membrane by fusion to a myristoylation sequence, we observed an increase in membrane recruitment of the SWC, protrusion velocity and cell migration. Together these data suggest that, in addition to its classical role in membrane trafficking, CHC brings the SWC to the plasma membrane, thereby controlling lamellipodium formation.
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