Intracellular and viral membrane fusion: A uniting mechanism Journal Article


Author: Söllner, T. H.
Article Title: Intracellular and viral membrane fusion: A uniting mechanism
Abstract: Structural and functional analyses have revealed remarkable mechanistic similarities between viral and intracellular fusion. Both fusion processes are driven by an orchestrated cascade of protein binding and folding reactions. After an initial tethering step, activation of the fusion machinery links the opposing membranes and protein folding pulls the membranes in close proximity; fusion pores form, open and dilate, and the process culminates in the complete merging of the lipid bilayers. Viral fusion is mediated by a single fusion protein, whereas the intracellular fusion machinery is split into matching halves, the v- and t-SNAREs. SNAREs, together with synaptotagmins, emerge as the key machinery for regulated exocytosis.
Keywords: protein expression; review; nonhuman; protein analysis; animals; models, biological; membrane glycoproteins; dimerization; protein structure, tertiary; molecular interaction; protein folding; protein structure; protein structure, secondary; viral matrix proteins; lipid bilayers; cell fusion; influenza virus; exocytosis; viral fusion proteins; vesicular transport proteins; acari; virus glycoprotein; membrane fusion; transmembrane domain; viral envelope proteins; snare proteins; virus envelope; intracellular membrane; hemagglutinin glycoproteins, influenza virus; snare; virus fusion protein; humans; priority journal; ha; haemagglutinin; n-ethylmaleimide-sensitive factor; nsf; semliki forest virus; sfv; snap; snap receptor; soluble nsf attachment protein; tbev; tick-borne encephalitis virus; tmd; influenza virus hemagglutinin; rabbit fibroma virus
Journal Title: Current Opinion in Cell Biology
Volume: 16
Issue: 4
ISSN: 0955-0674
Publisher: Elsevier Inc.  
Date Published: 2004-08-01
Start Page: 429
End Page: 435
Language: English
DOI: 10.1016/j.ceb.2004.06.015
PROVIDER: scopus
PUBMED: 15261676
DOI/URL:
Notes: Curr. Opin. Cell Biol. -- Cited By (since 1996):87 -- Export Date: 16 June 2014 -- CODEN: COCBE -- Source: Scopus
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  1. Thomas H Sollner
    65 Sollner