Abstract
The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, α-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all α-SNAP-containing complexes, only the α-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more α-SNAP but did not stimulate the ATPase of NSF. Copyright (C) 1998 Federation of European Biochemical Societies.
Original language | English |
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Pages (from-to) | 211-214 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 435 |
Issue number | 2-3 |
DOIs | |
State | Published - Sep 18 1998 |
Bibliographical note
Funding Information:We thank Dr. Susan A. Buhrow and Dr. Sergey V. Matveev for critical reading of the manuscript, Mr. Jim Smith for his excellent photographic assistance, and the members of the Whiteheart laboratory for their invaluable discussion. We would also like to thank Dr. Phyllis Hanson for the generous gift of the synaptobrevin-2 (Vamp-2) expression construct. This work was supported by the National Institutes of Health Grant HL56652 (to S.W.W.).
Keywords
- AAA ATPase
- Membrane fusion
- N-Ethylmaleimide sensitive factor
- SNAP receptor
- Soluble NSF attachment protein
- Vesicular traffic
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology