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Published Online August 7, 2008
Science DOI: 10.1126/science.1161070

Reports

Submitted on May 28, 2008
Accepted on July 24, 2008

Helical Structures of ESCRT-III Are Disassembled by VPS4

Suman Lata 1, Guy Schoehn 2, Ankur Jain 3, Ricardo Pires 1, Jacob Piehler 4, Heinrich G. Göttlinger 5, Winfried Weissenhorn 1*

1 Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.
2 Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.; Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CEA-CNRS-UJF, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
3 Institute of Biochemistry, Johann Wolfgang Goethe-University, Max-von-Laue Str. 9, 60438 Frankfurt am Main, Germany.; Present address: Department of Physics, University of Illinois, 1110 W. Green Street, Urbana, IL 61801, USA.
4 Institute of Biochemistry, Johann Wolfgang Goethe-University, Max-von-Laue Str. 9, 60438 Frankfurt am Main, Germany.
5 Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.

* To whom correspondence should be addressed.
Winfried Weissenhorn , E-mail: weissenhorn{at}embl.fr

During intracellular membrane trafficking and remodeling, protein complexes known as the ESCRTs interact with membranes and are required for budding processes directed away from the cytosol, including the budding of intralumenal vesicles to form multivesicular bodies, for the budding of some enveloped viruses, and for daughter cell scission in cytokinesis. Here, we found that the ESCRT-III subunits CHMP2A and CHMP3 could assemble in vitro into helical tubular structures that expose their membrane interaction sites on the outside of the tubule while the AAA-type ATPase VPS4 could bind on the inside of the tubule and disassemble the tubes upon ATP hydrolysis. CHMP2A and CHMP3 copolymerized in solution, and their membrane targeting was cooperatively enhanced on planar lipid bilayers. Such helical CHMP structures could thus assemble within the neck of an inwardly budding vesicle, catalyzing late steps in budding under the control of VPS4.


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