ArticleCell reports2016
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- A Highly Conserved SNARE-Associated Protein Enhances Plant Immunity by Regulating Vesicle Trafficking.Plant biotechnology journal · 2026Article
- A pathogenic mutation in α-SNAP impairs membrane lipid binding by concealing a critical hydrophobic loop.Communications biology · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Comparative effects of standardized Centella asiatica extract (ECa 233) and its active compound mixture on proteomics and mitochondrial function.Scientific reports · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Adherent junctions: Physiology, role in hydrocephalus and potential therapeutic targets.IBRO neuroscience reports · 2025Review
- Abnormal Transcytosis Mechanisms in the Pathogenesis of Hydrocephalus: A Review.International journal of molecular sciences · 2025Review
- After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.Molecular biology of the cell · 2024Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
- Trafficking in cancer: from gene deregulation to altered organelles and emerging biophysical properties.Frontiers in cell and developmental biology · 2024Review
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- Nano-Precision Tweezers for Mechanosensitive Proteins and Beyond.Molecules and cells · 2022Review
- Single-molecule manipulation of macromolecules on GUV or SUV membranes using optical tweezers.Biophysical journal · 2021Article
- Phosphatidylinositol and phosphatidylinositol-3-phosphate activate HOPS to catalyze SNARE assembly, allowing small headgroup lipids to support the terminal steps of membrane fusion.Molecular biology of the cell · 2021Article
- Article
- Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes.Nature communications · 2021Article
- Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.eLife · 2021Article
- De novo variants in SNAP25 cause an early-onset developmental and epileptic encephalopathy.Genetics in medicine : official journal of the American College of Medical Genetics · 2021Article
- A pathogenesis-related protein GmPR08-Bet VI promotes a molecular interaction between the GmSHMT08 and GmSNAP18 in resistance to Heterodera glycines.Plant biotechnology journal · 2020Article
- Munc18-1 is crucial to overcome the inhibition of synaptic vesicle fusion by αSNAP.Nature communications · 2019Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Recent experiments showed that α-SNAP also dramatically enhances SNARE assembly and membrane fusion. How α-SNAP is involved in these opposing activities is not known. Here, we examine the effect of α-SNAP on the stepwise assembly of the synaptic SNARE complex using optical tweezers. We found that α-SNAP destabilized the linker domain (LD) of the SNARE complex but stabilized its C-terminal domain (CTD) through a conformational selection mechanism. In contrast, α-SNAP minimally affected assembly of the SNARE N-terminal domain (NTD), indicating that α-SNAP barely bound the partially assembled trans-SNARE complex. Thus, α-SNAP recognizes the folded CTD for SNARE disassembly with NSF and subtly modulates membrane fusion by altering the stabilities of the SNARE CTD and LD.
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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.