| Primary Identifier | IPR027641 | Type | Family |
| Short Name | WASP |
| description | This entry represents the Actin nucleation-promoting factor WAS (WASP). The WASP proteins signal to the cytoskeleton through the Arp2/3 complex, an actin-nucleating assembly that regulates the structure and dynamics of actin filament networks at the leading edge of the cell []. The activity of WASP can be regulated by the Rho-family GTPase, Cdc42 []. Mutations in WASP lead to the Wiskott-Aldrich syndrome, a paediatric disorder characterised by actin cytoskeletal defects in haematopoietic cells, leading clinically to thrombocytopenia, eczema and immunodeficiency [].Similar to mammalian WASP proteins, Wsp1 and Las17 also has a role in regulating actin assembly [, ]. In Saccharomyces cerevisiae, Las17 is the primary activator of Arp2/3-driven actin nucleation and is required for membrane invagination during endocytosis []. Las17 can also nucleate actin filaments independently of Arp2/3 through its polyproline domain [].WASP family members have unique N-terminal regions, followed by a central segment rich in proline, and a common C-terminal region. Their conserved C-terminal VCA domain consists of two WH2 (WASP homology 2) domains ("V"referring to either a single or multiple WH2 domains), followed by a connector domain ("C") and an acidic short extension ("A"). In the VCA region, the WH2 domain(s) bind G-actin, whereas the CA domain binds Arp2/3 complex []. Their distinct N-terminal region enables family members to activate Arp2/3 in response to differentupstream signals. |
