Ontology highlight
ABSTRACT:
SUBMITTER: Helfer E
PROVIDER: S-EPMC1422163 | biostudies-literature | 2006 Mar
REPOSITORIES: biostudies-literature
Helfer Emmanuèle E Nevalainen Elisa M EM Naumanen Perttu P Romero Stéphane S Didry Dominique D Pantaloni Dominique D Lappalainen Pekka P Carlier Marie-France MF
The EMBO journal 20060302 6
Twinfilins are conserved actin-binding proteins composed of two actin depolymerizing factor homology (ADF-H) domains. Twinfilins are involved in diverse morphological and motile processes, but their mechanism of action has not been elucidated. Here, we show that mammalian twinfilin both sequesters ADP-G-actin and caps filament barbed ends with preferential affinity for ADP-bound ends. Twinfilin replaces capping protein and promotes motility of N-WASP functionalized beads in a biomimetic motility ...[more]