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Overview
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Background
Wiskostatin is an N-WASP inhibitor, with an IC50 value slightly less than 10 μM. Wiskostatin interacts with a cleft in the regulatory GTPase-binding domain (GBD) of N-WASP and maintains N-WASP in an inactive conformation, thereby inhibiting Cdc42 and phosphatidylinositol 4,5-bisphosphate (PIP2) mediated N-WASP activation, as well as Arp2/3 complex activation. N-WASP, highly expressed in the brain, belongs to the WASP family in which member proteins initiate the nucleation of new actin filaments through activation of the Arp2/3 complex, and thus are emerging as critical regulators of the actin cytoskeleton. By inhibiting N-WASP, wiskostatin has been shown to interfere with the formation of dendritic spines and synapses in neurons.
1. Peterson JR, Bickford LC, Morgan D, et al. Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation. Nature Structural & Molecular Biology, 2004, 11(8): 747-755.
2. Wegner AM, Nebhan CA, Hu L, et al. N-wasp and the arp2/3 complex are critical regulators of actin in the development of dendritic spines and synapses. Journal of Biological Chemistry, 2008, 283(23): 15912-15920.
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