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].
3D Structures of Wiskott-Aldrich syndrome protein
Wiskott-Aldrich syndrome protein 3D structures
References
- ↑ Westerberg LS, Dahlberg C, Baptista M, Moran CJ, Detre C, Keszei M, Eston MA, Alt FW, Terhorst C, Notarangelo LD, Snapper SB. Wiskott-Aldrich syndrome protein (WASP) and N-WASP are critical for peripheral B-cell development and function. Blood. 2012 Apr 26;119(17):3966-74. doi: 10.1182/blood-2010-09-308197. Epub 2012 , Mar 12. PMID:22411869 doi:http://dx.doi.org/10.1182/blood-2010-09-308197
- ↑ Suzuki T, Mimuro H, Suetsugu S, Miki H, Takenawa T, Sasakawa C. Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading. Cell Microbiol. 2002 Apr;4(4):223-33. PMID:11952639
- ↑ Notarangelo LD, Miao CH, Ochs HD. Wiskott-Aldrich syndrome. Curr Opin Hematol. 2008 Jan;15(1):30-6. PMID:18043243 doi:http://dx.doi.org/10.1097/MOH.0b013e3282f30448
