Molecular mechanism of Ena/VASP-mediated actin-filament elongation

• Dennis Breitsprecher ^[1] ; Antje K Kiesewetter ^[1] ; Joern Linkner ^[1] ; Marlene Vinzenz ^[2] ; Theresia E B Stradal ^[4] ; John Victor Small ^[2] ; Ute Curth ^[1] ; Richard B Dickinson ^[3] ; Jan Faix ^[1]
  1. [1] Hannover Medical School

     Hannover Medical School

     Region Hannover, Alemania

     
  2. [2] Institute of Molecular Biotechnology

     Institute of Molecular Biotechnology

     Innere Stadt, Austria

     
  3. [3] University of Florida

     University of Florida

     Estados Unidos

     
  4. [4] Signaling and Motility Group, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany; Institute for Molecular Cell Biology, University of Münster, Münster, Germany

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• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 30, Nº. 3, 2011, págs. 456-467
• Idioma: inglés
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• Resumen

  • Ena/VASP proteins have important functions in actin-dependent processes. A model for the actin elongation activity of Ena/VASP based on the affinity and saturation state of WH2-domain-mediated actin monomer binding is presented.