Reference : Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/6268
Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement
English
Giganti, A. [Lab. de Biol. Molec. d'Analyse Gen., Centre de Recherche Public-Sante, 42 rue du Laboratorie, L-1911 Luxembourg, Luxembourg]
Plastino, J. [Laboratoire Physicochimie 'Curie', UMR168 CNRS/Institut Curie, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France]
Janji, B. [Lab. de Biol. Molec. d'Analyse Gen., Centre de Recherche Public-Sante, 42 rue du Laboratorie, L-1911 Luxembourg, Luxembourg]
Van Troys, M. [Department of Biochemistry, Faculty of Medicine/Health Sciences, Ghent University, Ghent, Belgium]
Lentz, D. [Lab. de Biol. Molec. d'Analyse Gen., Centre de Recherche Public-Sante, 42 rue du Laboratorie, L-1911 Luxembourg, Luxembourg]
Ampe, C. [Department of Biochemistry, Faculty of Medicine/Health Sciences, Ghent University, Ghent, Belgium]
Sykes, C. [Laboratoire Physicochimie 'Curie', UMR168 CNRS/Institut Curie, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
2005
Journal of Cell Science
Company of Biologists
118
6
1255-1265
Yes (verified by ORBilu)
International
0021-9533
1477-9137
Cambridge
United Kingdom
[en] ADF ; Bundling ; CH domain ; Cofilin ; Nucleation ; T-Fimbrin ; F actin ; Wiskott Aldrich syndrome protein ; Actin Depolymerizing Factors ; Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins ; Animals ; Antibodies, Monoclonal ; Calcium ; Cell Membrane ; Cell-Free System ; Cercopithecus aethiops ; Cross-Linking Reagents ; Cytoskeletal Proteins ; DNA ; Electrophoresis, Polyacrylamide Gel ; Hela Cells ; Humans ; Microfilament Proteins ; Microfilaments ; Microscopy, Fluorescence ; Microscopy, Phase-Contrast ; Neoplasm Proteins ; Phosphoproteins ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Time Factors ; Transfection ; Vero Cells ; Wiskott-Aldrich Syndrome Protein ; Animalia ; Vespidae
[en] 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.
http://hdl.handle.net/10993/6268
10.1242/jcs.01698

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