ArticleThe Journal of biological chemistry2015
Three αSNAP and 10 ATP molecules are used in SNARE complex disassembly by N-ethylmaleimide-sensitive factor (NSF).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Specialized high-capacity mitochondria fuel cell invasion.Current biology : CB · 2026Article
- Mitochondria-ER contact site components regulate the formation and localization of specialized high-capacity mitochondria in themicroPublication biology · 2025Article
- The C. elegans anchor cell: A model to elucidate mechanisms underlying invasion through basement membrane.Seminars in cell & developmental biology · 2024Review
- Localized glucose import, glycolytic processing, and mitochondria generate a focused ATP burst to power basement-membrane invasion.Developmental cell · 2022Article
- Fueling Cell Invasion through Extracellular Matrix.Trends in cell biology · 2021Review
- Article
- NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.eLife · 2018Article
- Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017Review
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
- Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF).Journal of molecular biology · 2016Review
- α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle.Cell reports · 2016Article
- Three steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex.Current opinion in chemical biology · 2015Review
- Cryo-EM structure of SNAP-SNARE assembly in 20S particle.Cell research · 2015Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The fusion of intracellular membranes is driven by the formation of a highly stable four-helix bundle of SNARE proteins embedded in the vesicle and target membranes. N-Ethylmaleimide sensitive factor recycles SNAREs after fusion by binding to the SNARE complex through an adaptor protein, αSNAP, and using the energy of ATP hydrolysis to disassemble the complex. Although only a single molecule of αSNAP binds to a soluble form of the SNARE complex, we find that three molecules of αSNAP are used for SNARE complex disassembly. We describe an engineered αSNAP trimer that supports more efficient SNARE complex disassembly than monomeric αSNAP. Using the trimerized αSNAP, we find that N-ethylmaleimide-sensitive factor hydrolyzes 10 ATP molecules on average to disassemble a single SNARE complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.