Wiskott-Aldrich syndrome protein

Function

Wiskott-Aldrich syndrome protein (WASP) is involved in nucleating of new F-actin. In the autoinhibited form of WASP a region of the N-terminal interacts with a region of its C-terminal. This interaction is disrupted by CDC42 and phosphatidylinositol 4,5-bisphosphate (PIP2) resulting in the active WASP. WASP domains include EVH1 domain in the N-terminal which bind proline-rich sequences in the WASP-interacting proteins; WH2 domain is ca. 18 residues long and interacts with actin; CRIB or GTPase-binding domain which interacts with CDC42. N-WASP (Neural WASP) belongs to the WASP family of proteins. Human N-WASP stimulates the actin-nucleating activity^[1].

Relevance

N-WASP induces actin polymerization in the Shigella bacterium^[2]. This bacterium causes dysentery.

Disease

Mutations in WASP can cause Wiskott-Aldrich syndrome which is a rare inherited disease characterized by immune disregulation^[3].