Journal
SCIENCE
Volume 321, Issue 5894, Pages 1354-1357Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1161070
Keywords
-
Categories
Funding
- Deutsche Forschungsgemeinschaft [SPP 1175]
- Agence Nationale de la Recherche sur le SIDA
- Universite Joseph Fourier
- Agence Nationale de la Recherche
- CNRS
- NIH [AI29873]
- European Molecular Biology Organization
- International Human Frontier Science Program Organization
Ask authors/readers for more resources
During intracellular membrane trafficking and remodeling, protein complexes known as the ESCRTs ( endosomal sorting complexes required for transport) 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. We found that the ESCRT- III proteins CHMP2A and CHMP3 ( charged multivesicular body proteins 2A and 3) could assemble in vitro into helical tubular structures that expose their membrane interaction sites on the outside of the tubule, whereas the AAA- type adenosine triphosphatase VPS4 could bind on the inside of the tubule and disassemble the tubes upon adenosine triphosphate 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available