ArticleCell research2015
Cryo-EM structure of SNAP-SNARE assembly in 20S particle.
Article in Cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- A pathogenic mutation in α-SNAP impairs membrane lipid binding by concealing a critical hydrophobic loop.Communications biology · 2026Article
- Economical and Versatile Subunit Design Principles for Self-Assembled DNA Origami Structures.ACS nano · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Single-molecule two- and three-colour FRET studies reveal a transition state in SNARE disassembly by NSF.Nature communications · 2025Article
- DynaMight: estimating molecular motions with improved reconstruction from cryo-EM images.Nature methods · 2024Article
- Host antiviral factors hijack furin to block SARS-CoV-2, ebola virus, and HIV-1 glycoproteins cleavage.Emerging microbes & infections · 2023Review
- NSF/αSNAP2-mediated cis-SNARE complex disassembly precedes vesicle fusion in Arabidopsis cytokinesis.Nature plants · 2023Article
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- Perspective: Emerging strategies for determining atomic-resolution structures of macromolecular complexes within cells.Journal of structural biology · 2022Article
- Conquer by cryo-EM without physically dividing.Biochemical Society transactions · 2021Review
- Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes.Nature communications · 2021Article
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- Multi-body Refinement of Cryo-EM Images in RELION.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Article
- Review
- Hyper-Molecules: on the Representation and Recovery of Dynamical Structures for Applications in Flexible Macro-Molecules in Cryo-EM.Inverse problems · 2020Article
- Analysis of discrete local variability and structural covariance in macromolecular assemblies using Cryo-EM and focused classification.Ultramicroscopy · 2019Article
- Nanomachinery Organizing Release at Neuronal and Ribbon Synapses.International journal of molecular sciences · 2019Review
- Mechanistic insights into the SNARE complex disassembly.Science advances · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-ethylmaleimide-sensitive factor (NSF) and α soluble NSF attachment proteins (α-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular membrane fusion. To understand the disassembly mechanism of the SNARE complex by NSF and α-SNAP, we performed single-particle cryo-electron microscopy analysis of 20S particles and determined the structure of the α-SNAP-SNARE assembly portion at a resolution of 7.35 Å. The structure illustrates that four α-SNAPs wrap around the single left-handed SNARE helical bundle as a right-handed cylindrical assembly within a 20S particle. A conserved hydrophobic patch connecting helices 9 and 10 of each α-SNAP forms a chock protruding into the groove of the SNARE four-helix bundle. Biochemical studies proved that this structural element was critical for SNARE complex disassembly. Our study suggests how four α-SNAPs may coordinate with the NSF to tear the SNARE complex into individual proteins.
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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.