A novel actin-binding motif in Las17/WASP nucleates actin filaments independently of Arp2/3.

Actin nucleation is the key rate-limiting step in actin polymerization, and tight regulation of this process is critical to ensure that actin filaments form only at specific regions of the cell. Las17 is the primary activator of Arp2/3-driven actin nucleation in yeast and is required for membrane invagination during endocytosis. Its mammalian homolog, WASP, has also been studied extensively as an activator of Arp2/3-driven actin polymerization. In both Las17 and WASP, actin nucleation activity is attributed to an ability to bind actin through a WH2 domain and to bind Arp2/3 through an acidic region. The central region of both Las17 and WASP is rich in proline residues and is generally considered to bind to SH3-domain-containing proteins.

Pubmed ID: 23290554 RIS Download