| WAS Protein | |
|---|---|
| Gene | [WAS](/entities/was) (Wiskott-Aldrich Syndrome) |
| UniProt ID | [P42768](https://www.uniprot.org/uniprot/P42768) |
| Alternative Names | Wiskott-Aldrich Syndrome Protein, WASp |
| Molecular Weight | 52 kDa |
| Subcellular Localization | Cytosol, plasma membrane |
| Protein Family | Wiskott-Aldrich syndrome protein family |
| PDB Structures | [1EJ5](https://www.ebi.ac.uk/pdbe/entry/pdb/1ej5), [1I2X](https://www.ebi.ac.uk/pdbe/entry/pdb/1i2x) |
WAS Protein (WASp) is a member of the Wiskott-Aldrich syndrome protein family that regulates actin cytoskeleton remodeling through activation of the Arp2/3 complex. It links signaling pathways to actin polymerization, playing crucial roles in immune cell function and neuronal development. Mutations in the WAS gene cause Wiskott-Aldrich syndrome, an X-linked immunodeficiency characterized by eczema, thrombocytopenia, and increased risk of autoimmunity and lymphoma[1].
WASp contains multiple functional domains:
WASp exists in an autoinhibited conformation where the VCA domain is masked[2].
In the nervous system, WASp is involved in:
WAS-targeted strategies include:
Gene therapy for WAS has shown promising results in clinical trials[4].
Thrasher. WASp in immune cell function (2009). Nature Reviews Immunology.
Symons et al. WASp structure and function (1996). Proceedings of the National Academy of Sciences.
Notarangelo. Clinical spectrum of WAS (2010). Journal of Allergy and Clinical Immunology.
Thrasher. WASp in immunity and beyond. Nature Reviews Immunology. 2009. ↩︎
Symons et al. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42. Proceedings of the National Academy of Sciences. 1996. ↩︎
Notarangelo. Immunodeficiency and immune dysregulation. Journal of Allergy and Clinical Immunology. 2010. ↩︎
Cavazzana-Calvo. Gene therapy for WAS. Blood. 2014. ↩︎