SNAREpins are functionally resistant to disruption by NSF and αSNAP Journal Article


Authors: Weber, T.; Parlati, F.; Mcnew, J. A.; Johnston, R. J.; Westermann, B.; Söllner, T. H.; Rothman, J. E.
Article Title: SNAREpins are functionally resistant to disruption by NSF and αSNAP
Abstract: SNARE (SNAP [soluble NSF {N-ethylmaleimide-sensitive fusion protein} attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by the action of the abundant cytoplasmic ATPase NSF, which is necessary to maintain a supply of uncombined v- and t- SNAREs for fusion in cells. Fusion is mediated by these same SNARE proteins, forming trans-SNARE complexes between membranes. This raises an important question: why doesn't NSF disrupt these SNARE complexes as well, preventing fusion from occurring at all? Here, we report several lines of evidence that demonstrate that SNAREpins (trans-SNARE complexes) are in fact functionally resistant to NSF, and they become so at the moment they form and commit to fusion. This elegant design allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption.
Keywords: protein conformation; animals; mice; cells, cultured; gene expression; protein assembly; membrane proteins; gene function; regulatory mechanism; gene disruption; carrier proteins; temperature; protein structure, tertiary; rats; adenosine triphosphate; mutagenesis; liposomes; lipid bilayers; cell fusion; membrane vesicle; vesicular transport proteins; intracellular membranes; membrane fusion; membrane structure; snare protein; qa-snare proteins; r-snare proteins; snare proteins; snare; priority journal; article; nsf; n-ethylmaleimide-sensitive proteins; soluble n-ethylmaleimide-sensitive factor attachment proteins; αsnap
Journal Title: Journal of Cell Biology
Volume: 149
Issue: 5
ISSN: 0021-9525
Publisher: Rockefeller University Press  
Date Published: 2000-05-29
Start Page: 1063
End Page: 1072
Language: English
DOI: 10.1083/jcb.149.5.1063
PUBMED: 10831610
PROVIDER: scopus
PMCID: PMC2174819
DOI/URL:
Notes: Export Date: 18 November 2015 -- Source: Scopus
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MSK Authors
  1. Thomas H Sollner
    65 Sollner
  2. James E Rothman
    120 Rothman
  3. Thomas Weber
    14 Weber
  4. James A Mcnew
    21 McNew
  5. Francesco Parlati
    17 Parlati