Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains.
Cell
; 128(5): 901-13, 2007 Mar 09.
Article
em En
| MEDLINE
| ID: mdl-17350575
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Citoesqueleto de Actina
/
Membrana Celular
/
Actinas
/
Proteína Neuronal da Síndrome de Wiskott-Aldrich
Limite:
Animals
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article