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J. Biol. Chem., Vol. 282, Issue 46, 33599-33608, November 16, 2007

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The LIM Domains of WLIM1 Define a New Class of Actin Bundling Modules^*

Clément Thomas¹, Flora Moreau, Monika Dieterle, Céline Hoffmann, Sabrina Gatti, Christina Hofmann, Marleen Van Troys^¶, Christophe Ampe^¶, and André Steinmetz

From the Centre de Recherche Public-Santé, Luxembourg, L-1526 Luxembourg, the Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique, F-67084 Strasbourg, France, and the ^¶VIB Department of Medical Protein Research, Ugent and Department of Biochemistry, Faculty of Medicine and Health Sciences, B-9052 Ghent, Belgium

Actin filament bundling, i.e. the formation of actin cables, is an important process that relies on proteins able to directly bind and cross-link subunits of adjacent actin filaments. Animal cysteine-rich proteins and their plant counterparts are two LIM domain-containing proteins that were recently suggested to define a new family of actin cytoskeleton regulators involved in actin filament bundling. We here identified the LIM domains as responsible for F-actin binding and bundling activities of the tobacco WLIM1. The deletion of one of the two LIM domains reduced significantly, but did not entirely abolish, the ability of WLIM1 to bind actin filaments. Individual LIM domains were found to interact directly with actin filaments, although with a reduced affinity compared with the native protein. Variants lacking the C-terminal or the inter-LIM domain were only weakly affected in their F-actin stabilizing and bundling activities and trigger the formation of thick cables containing tightly packed actin filaments as does the native protein. In contrast, the deletion of one of the two LIM domains negatively impacted both activities and resulted in the formation of thinner and wavier cables. In conclusion, we demonstrate that the LIM domains of WLIM1 are new autonomous actin binding and bundling modules that cooperate to confer WLIM1 high actin binding and bundling activities.

Received for publication, May 4, 2007 , and in revised form, September 6, 2007.

^* This work was supported by the Ministry of Culture, Higher Education and Research and the National Research Fund (Luxembourg). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 352-26970-253; Fax: 352-26970-390; E-mail: clement.thomas{at}crp-sante.lu.

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