Journal
CELL
Volume 128, Issue 5, Pages 901-913Publisher
CELL PRESS
DOI: 10.1016/j.cell.2006.12.049
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Funding
- NEI NIH HHS [PN2 EY016546, PN2 EY 016546] Funding Source: Medline
- NIGMS NIH HHS [R01 GM066229-05, GM 066229, R01 GM066229] Funding Source: Medline
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Actin filament networks exert protrusive and attachment forces on membranes and thereby drive membrane deformation and movement. Here, we show that N-WASP WH2 domains play a previously unanticipated role in vesicle movement by transiently attaching actin filament barbed ends to the membrane. To dissect the attachment mechanism, we reconstituted the propulsive motility of lipid-coated glass beads, using purified soluble proteins. N-WASP WH2 mutants assembled actin comet tails and initiated movement, but the comet tails catastrophically detached from the membrane. When presented on the surface of a lipid-coated bead, WH2 domains were sufficient to maintain comet tail attachment. In v-Src-transformed fibroblasts, N-WASP WH2 mutants were severely defective in the formation of circular podosome arrays. In addition to creating an attachment force, interactions between WH2 domains and barbed ends may locally amplify signals for dendritic actin nucleation.
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