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

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Title
Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes
Author(s)
Ryu J.-K.; Jahn R.; Tae-Young Yoon
Publication Date
2016-08
Journal
BIOPOLYMERS, v.105, no.8, pp.518 - 531
Publisher
WILEY-BLACKWELL
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 (AAA+ proteins). AAA+ 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 AAA+ ATPases. © 2016 Wiley Periodicals, Inc
URI
https://pr.ibs.re.kr/handle/8788114/2636
ISSN
0006-3525
Appears in Collections:
Center for Nanomedicine (나노의학 연구단) > Journal Papers
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