Document Detail

Protein-driven membrane stresses in fusion and fission.
MedLine Citation:
PMID:  20638285     Owner:  NLM     Status:  MEDLINE    
Cellular membranes undergo continuous remodeling. Exocytosis and endocytosis, mitochondrial fusion and fission, entry of enveloped viruses into host cells and release of the newly assembled virions, cell-to-cell fusion and cell division, and budding and fusion of transport carriers all proceed via topologically similar, but oppositely ordered, membrane rearrangements. The biophysical similarities and differences between membrane fusion and fission become more evident if we disregard the accompanying biological processes and consider only remodeling of the lipid bilayer. The forces that determine the bilayer propensity to undergo fusion or fission come from proteins and in most cases from membrane-bound proteins. In this review, we consider the mechanistic principles underlying the fusion and fission reactions and discuss the current hypotheses on how specific proteins act in the two types of membrane remodeling.
Michael M Kozlov; Harvey T McMahon; Leonid V Chernomordik
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't; Review     Date:  2010-07-16
Journal Detail:
Title:  Trends in biochemical sciences     Volume:  35     ISSN:  0968-0004     ISO Abbreviation:  Trends Biochem. Sci.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-11-24     Completed Date:  2010-12-08     Revised Date:  2014-02-19    
Medline Journal Info:
Nlm Unique ID:  7610674     Medline TA:  Trends Biochem Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  699-706     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Ltd. All rights reserved.
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MeSH Terms
Cell Membrane / chemistry*,  metabolism*
Membrane Fusion*
Membrane Proteins / metabolism*
Grant Support
MC_U105178795//Medical Research Council; ZIA HD001501-21/HD/NICHD NIH HHS; //Medical Research Council
Reg. No./Substance:
0/Membrane Proteins

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