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  Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.

Ryu, J. K., Jahn, R., & Yoon, T. Y. (2016). Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes. Biopolymers, 105(8), 518-531. doi:10.1002/bip.22854.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-12A5-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-186B-9
Genre: Journal Article

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 Creators:
Ryu, J. K., Author
Jahn, R.1, Author              
Yoon, T. Y., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: NSF; SNARE; alpha-SNAP; AAA1; single molecule
 Abstract: N-ethylmaleimide sensitive factor (NSF) is a key protein of intracellular membrane traffic. NSF is a highly conserved protein belonging to the ATPases associated with other activities (AAA1 proteins). AAA1 share common domains and all transduce ATP hydrolysis into major conformational movements that are used to carry out conformational work on client proteins. Together with its cofactor SNAP, NSF is specialized on disassembling highly stable SNARE complexes that form after each membrane fusion event. Although essential for all eukaryotic cells, however, the details of this reaction have long been enigmatic. Recently, major progress has been made in both elucidating the structure of NSF/SNARE complexes and in understanding the reaction mechanism. Advances in both cryo EM and single molecule measurements suggest that NSF, together with its cofactor SNAP, imposes a tight grip on the SNARE complex. After ATP hydrolysis and phosphate release, it then builds up mechanical tension that is ultimately used to rip apart the SNAREs in a single burst. Because the AAA domains are extremely well-conserved, the molecular mechanism elucidated for NSF is presumably shared by many other AAA1 ATPases.

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Language(s): eng - English
 Dates: 2016-04-082016-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/bip.22854
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Title: Biopolymers
Source Genre: Journal
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Pages: - Volume / Issue: 105 (8) Sequence Number: - Start / End Page: 518 - 531 Identifier: -