Publication Date:
2008-08-09
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758909/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758909/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lata, Suman -- Schoehn, Guy -- Jain, Ankur -- Pires, Ricardo -- Piehler, Jacob -- Gottlinger, Heinrich G -- Weissenhorn, Winfried -- AI29873/AI/NIAID NIH HHS/ -- R37 AI029873/AI/NIAID NIH HHS/ -- R37 AI029873-20/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2008 Sep 5;321(5894):1354-7. doi: 10.1126/science.1161070. Epub 2008 Aug 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unit for Virus Host Cell Interaction, UMR 5233 UJF (Universite Joseph Fourier)-EMBL (European Molecular Biology Laboratory)-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18687924" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphatases/*metabolism
;
Adenosine Triphosphate/metabolism
;
Biomarkers, Tumor/*chemistry/*metabolism
;
Centrifugation, Density Gradient
;
Dimerization
;
Endosomal Sorting Complexes Required for Transport
;
Humans
;
Lipid Bilayers/chemistry
;
Models, Molecular
;
Protein Conformation
;
Protein Structure, Secondary
;
Unilamellar Liposomes/chemistry
;
Vesicular Transport Proteins/chemistry/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
