ArticleJournal of structural biology2012
Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly.
Article in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
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Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.
- Interruption of Endolysosomal Trafficking After Focal Brain Ischemia.Frontiers in molecular neuroscience · 2021Pooled it
- Article
- Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes.Nature communications · 2021Article
- Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF).Journal of molecular biology · 2016Review
- Association of Alpha-Soluble NSF Attachment Protein with Epileptic Seizure.Journal of molecular neuroscience : MN · 2015Article
- Cryo-EM structure of SNAP-SNARE assembly in 20S particle.Cell research · 2015Article
- Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.Science (New York, N.Y.) · 2015Article
- The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.Journal of molecular biology · 2015Article
- Article
- Three αSNAP and 10 ATP molecules are used in SNARE complex disassembly by N-ethylmaleimide-sensitive factor (NSF).The Journal of biological chemistry · 2015Article
- Ganglioside regulation of AMPA receptor trafficking.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Processive ATP-driven substrate disassembly by the N-ethylmaleimide-sensitive factor (NSF) molecular machine.The Journal of biological chemistry · 2013Article
- The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Homohexameric, N-Ethylmaleimide Sensitive Factor (NSF) disassembles Soluble NSF Attachment Protein Receptor (SNARE) complexes after membrane fusion, an essential step in vesicular trafficking. NSF contains three domains (NSF-N, NSF-D1, and NSF-D2), each contributing to activity. We combined electron microscopic (EM) analysis, analytical ultracentrifugation (AU) and functional mutagenesis to visualize NSF's ATPase cycle. 3D density maps show that NSF-D2 remains stable, whereas NSF-N undergoes large conformational changes. NSF-Ns splay out perpendicular to the ADP-bound hexamer and twist upwards upon ATP binding, producing a more compact structure. These conformations were confirmed by hydrodynamic, AU measurements: NSF-ATP sediments faster with a lower frictional ratio (f/f(0)). Hydrodynamic analyses of NSF mutants, with specific functional defects, define the structures underlying these conformational changes. Mapping mutations onto our 3D models allows interpretation of the domain movement and suggests a mechanism for NSF binding to and disassembly of SNARE complexes.
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Registered trials
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