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Vol. 11, Issue 10, 3485-3494, October 2000

Vimentin Filaments in Fibroblasts Are a Reservoir for SNAP23, a Component of the Membrane Fusion Machinery

Wolfgang Faigle,* Emma Colucci-Guyon,dagger Daniel Louvard,Dagger Sebastian Amigorena,* and Thierry Gallidagger §||

 *Group of Cellular Biology of Tumoral Immunity, Institut National de la Santé et de la Recherche Médicale U520, Institut Curie, F-75248 Paris Cédex 05, France;  Dagger Group of Membrane Traffic and Neuronal Plasticity, Institut National de la Santé et de la Recherche Médicale U536, Institut Curie, F-75248 Paris Cédex 05, France;  §Group of Morphogenesis and Cell Signalling, Centre National de la Recherche Scientifique Unite Mixte de Recherche 144, Institut Curie, F-75248 Paris Cédex 05, France; and  dagger Unité de Biologie du Développement, Institut Pasteur, Centre National de la Recherche Scientifique Unité de Recherche Associée 1960, 75724 Paris Cédex 15, France

Soluble N-ethyl maleimide-sensitive fusion protein attachment protein receptors (SNAREs) are core machinery for membrane fusion during intracellular vesicular transport. Synaptosome-associated protein of 23 kDa (SNAP23) is a target SNARE previously identified at the plasma membrane, where it is involved in exocytotic membrane fusion. Here we show that SNAP23 associates with vimentin filaments in a Triton X-100 insoluble fraction in fibroblasts in primary culture and HeLa cells. Upon treatment of human fibroblasts with N-ethyl-maleimide, SNAP23 dissociates from vimentin filaments and forms a protein complex with syntaxin 4, a plasma membrane SNARE. The vimentin-associated pool of SNAP23 can therefore be a reservoir, which would supply the plasma membrane fusion machinery, in fibroblasts. Our observation points to a yet unexplored role of intermediate filaments.


|| Corresponding author: E-mail address: thierry.galli{at}curie.fr.


Molecular Biology of the Cell
Vol. 11, 3485-3494, October 2000
Copyright © 2000 by The American Society for Cell Biology



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