Neural Wiskott-Aldrich syndrome protein (IPR030214)

Short name: N-WASP

Overlapping homologous superfamilies


Family relationships



The neural Wiskott-Aldrich syndrome (N-WASP) protein belongs to the WASP family, whose members 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 [PMID: 18650809]. 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 [PMID: 22847007]. Their distinct N-terminal region enables family members to activate Arp2/3 in response to different upstream signals.

Interestingly, pathogen such as Enteropathogenic Escherichia coli can affect host cell Arp2/3-dependent actin assembly through injecting a bacterial protein, translocated intimin receptor (Tir), into the host cell [PMID: 22966049, PMID: 23707428]. Tir binds to the host-cell adaptor protein Nck. Nck interacts with a complex of WIP and N-WASP, resulting in the activation of the Arp2/3 complex and actin polymerisation [PMID: 24284073]. Vaccinia virus can also affect actin assembly in the host cells through the interaction between its transmembrane protein A36 and host proteins, such as Grb2, Nck, WIP and N-WASP. Arp2/3-induced actin polymerisation propels the virus away from the cell surface towards neighbouring cells, enhancing the spread of infection [PMID: 24284073].

GO terms

Biological Process

GO:0007015 actin filament organization
GO:2000601 positive regulation of Arp2/3 complex-mediated actin nucleation

Molecular Function

GO:0003779 actin binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.