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The WASP-Homology 2 Domain and Cytoskeleton Assembly

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Actin-based Motility

Abstract

One of the most abundant and functionally diverse actin-binding folds is the WASP homology 2 (WH2 or W) domain. The W domain is found in proteins involved in actin monomer sequestration and cytoskeleton scaffolding, but is particularly abundant among proteins that mediate the de novo formation of actin filaments, which includes actin filament nucleation and elongation factors. Known filament nucleators include the Arp2/3 complex and its large family of Nucleation Promoting Factors (NPFs), formins, Spire, Cobl, VopL/VopF, TARP and Lmod. These molecules are generally unrelated, but with the exception of formins they all use the W domain for interaction with actin. A common architecture, found in Spire, Cobl and VopL/VopF, consists of tandem W domains that bind three to four actin subunits to form a nucleus. Structural considerations suggest that NPFs-Arp2/3 complex can also be viewed as a specialized form of tandem W-based nucleator. Ena/VASP proteins are distantly related to WASP-family NPFs, and function as dedicated filament elongation factors among W-based nucleators.

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Acknowledgement

Supported by NIH grants GM073791.

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  1. Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, Philadelphia, PA, 19104-6085, USA

    Roberto Dominguez

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  1. Roberto Dominguez
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Correspondence to Roberto Dominguez .

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  1. , Laboratory of Structural Enzymology and, CNRS, Gif-sur-Yvette Cedex, 91198, France

    Marie-France Carlier

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Dominguez, R. (2010). The WASP-Homology 2 Domain and Cytoskeleton Assembly. In: Carlier, MF. (eds) Actin-based Motility. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-9301-1_11

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