Rapid and efficient fusion of phospholipid vesicles by the α-helical core of a SNARE complex in the absence of an N-terminal regulatory domain

Francesco Parlati, Thomas Weber, James A. McNew, Benedikt Westermann, Thomas H. Söllner, James E. Rothman

Research output: Contribution to journalArticlepeer-review

221 Scopus citations

Abstract

A protease-resistant core domain of the neuronal SNARE complex consists of an α-helical bundle similar to the proposed fusogenic core of vital fusion proteins [Skehel, J. J. and Wiley, D. C. (1998) Cell 95, 871-874]. We find that the isolated core of a SNARE complex efficiently fuses artificial bilayers and does so faster than full length SNAREs. Unexpectedly, a dramatic increase in speed results from removal of the N-terminal domain of the t- SNARE syntaxin, which does not affect the rate of assembly of v-t SNARES. In the absence of this negative regulatory domain, the half-time for fusion of an entire population of lipid vesicles by isolated SNARE cores (≃10 min) is compatible with the kinetics of fusion in many cell types.

Original languageEnglish
Pages (from-to)12565-12570
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number22
DOIs
StatePublished - 26 Oct 1999
Externally publishedYes

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