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Cited by 797

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Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy

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Hanson, Phyllis I, Roth, Robyn, Morisaki, Hiroshi, Jahn, Reinhard, Heuser, John E·1997·Cell

Abstract

Using quick-freeze/deep-etch electron microscopy of recombinant proteins adsorbed to mica, we show that NSF, the oligomeric ATPase involved in membrane fusion, is a hollow 10 x 16 nm cylinder whose conformation depends upon nucleotide binding. Depleted of nucleotide, NSF converts to a "splayed" protease-sensitive conformation that reveals its subunit composition. NSF's synaptic membrane substrate, the ternary SNARE complex containing syntaxin, SNAP-25, and synaptobrevin, is a 4 x 14 nm rod with a "tail" at one end, corresponding to the N-terminus of syntaxin. Using epitope tags, antibodies, and maltose-binding protein markers, we find that syntaxin and synaptobrevin are aligned in parallel in the complex, with their membrane anchors located at the same end of the rod. This SNARE rod binds with alpha-SNAP to one end of the NSF cylinder to form an asymmetric "20S" complex. Together, these images suggest how NSF could dissociate the SNARE complex and how association and dissociation of the complex could be related to membrane fusion.

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Metadata

Authors
Hanson, P. I., Roth, R., Morisaki, H., Jahn, R., & Heuser, J. E.
Venue
Cell
Publisher
Elsevier BV
Published
1997-08
Volume
90
Issue
3
Pages
523-535
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2052999464
Cited by
797
References
1
FWCI
23.93
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80512-7
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Hanson, P. I., Roth, R., Morisaki, H., Jahn, R., & Heuser, J. E. (1997). Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy. Cell. https://doi.org/10.1016/s0092-8674(00)80512-7

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