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 |