title: Review: Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.
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. Biopolymers 105: 518-531, 2016.
authors.affiliation: Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Delft, CJ, 2628, the Netherlands.
authors.forename: Je-Kyung
authors.initials: JK
authors.lastname: Ryu
authors.affiliation: Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, 37077, Germany.
authors.forename: Reinhard
authors.initials: R
authors.lastname: Jahn
authors.affiliation: Center for Nanomedicine, Institute for Basic Science (IBS) and Y-IBS Institute, Yonsei University, Seoul, 03722, South Korea.
authors.forename: Tae-Young
authors.initials: TY
authors.lastname: Yoon
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D020285:Cryoelectron Microscopy; D006801:Humans; D006868:Hydrolysis; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D052066:N-Ethylmaleimide-Sensitive Proteins / Q000737:chemistry / Q000378:metabolism; D000072417:Protein Domains; D050600:SNARE Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D046912:Multiprotein Complexes; D050600:SNARE Proteins; D000255:Adenosine Triphosphate; D052066:N-Ethylmaleimide-Sensitive Proteins
keywords: AAA+; NSF; SNARE; single molecule; α-SNAP