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First published online 1 March 2005
doi: 10.1242/jcs.01698

Journal of Cell Science 118, 1255-1265 (2005)
Published by The Company of Biologists 2005
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Research Article

Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement

Adeline Giganti1, Julie Plastino2,*, Bassam Janji1,*, Marleen Van Troys3, Delphine Lentz1, Christophe Ampe3, Cécile Sykes2 and Evelyne Friederich1,{ddagger}

1 Laboratoire de Biologie Moléculaire, d'Analyse Génique et de Modélisation, Centre de Recherche Public-Santé, 42, rue du Laboratoire, L-1911, Luxembourg
2 Laboratoire Physicochimie `Curie', UMR168 CNRS/Institut Curie, 11, rue Pierre et Marie Curie, 75231 Paris Cedex 05, France
3 Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, and Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB09), Belgium

{ddagger} Author for correspondence (e-mail: Evelyne.Friederich{at}crp-sante.lu)

Accepted 30 December 2004

Increasing evidence suggests that actin cross-linking or bundling proteins might not only structure the cortical actin cytoskeleton but also control actin dynamics. Here, we analyse the effects of T-plastin/T-fimbrin, a representative member of an important actin-filament cross-linking protein by combining a quantitative biomimetic motility assay with biochemical and cell-based approaches. Beads coated with the VCA domain of the Wiskott/Aldrich-syndrome protein (WASP) recruit the actin-nucleating Arp2/3 complex, polymerize actin at their surface and undergo movement when placed in cell-free extracts. T-Plastin increased the velocity of VCA beads 1.5 times, stabilized actin comets and concomitantly displaced cofilin, an actin-depolymerizing protein. T-Plastin also decreased the F-actin disassembly rate and inhibited cofilin-mediated depolymerization of actin filaments in vitro. Importantly, a bundling-incompetent variant comprising the first actin-binding domain (ABD1) had similar effects. In cells, this domain induced the formation of long actin cables to which other actin-regulating proteins were recruited. Altogether, these results favor a mechanism in which binding of ABD1 controls actin turnover independently of cross-link formation. In vivo, this activity might contribute to the assembly and maintenance of the actin cytoskeleton of plasma-membrane protrusions.

Key words: T-Fimbrin, Bundling, CH domain, Nucleation, Cofilin, ADF


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© The Company of Biologists Ltd 2005