The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
SNARE-complex disassembly by NSF follows synaptic-vesicle fusion
Open accessAbstract
Soluble N- ethylmaleimide-sensitive fusion attachment protein receptor (SNARE)-mediated fusion of synaptic vesicles with the presynaptic-plasma membrane is essential for communication between neurons. Disassembly of the SNARE complex requires the ATPase N -ethylmaleimide-sensitive fusion protein (NSF). To determine where in the synaptic-vesicle cycle NSF functions, we have undertaken a genetic analysis of comatose (dNSF-1) in Drosophila . Characterization of 16 comatose mutations demonstrates that NSF mediates disassembly of SNARE complexes after synaptic-vesicle fusion. Hypomorphic mutations in NSF cause temperature-sensitive paralysis, whereas null mutations result in lethality. Genetic-interaction studies with para demonstrate that blocking evoked fusion delays the accumulation of assembled SNARE complexes and behavioral paralysis that normally occurs in comatose mutants, indicating NSF activity is not required in the absence of vesicle fusion. In addition, the entire vesicle pool can be depleted in shibire comatose double mutants, demonstrating that NSF activity is not required for the fusion step itself. Multiple rounds of vesicle fusion in the absence of NSF activity poisons neurotransmission by trapping SNAREs into cis-complexes. These data indicate that NSF normally dissociates and recycles SNARE proteins during the interval between exocytosis and endocytosis. In the absence of NSF activity, there are sufficient fusion-competent SNAREs to exocytose both the readily released and the reserve pool of synaptic vesicles.
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“Finally, the SNARE complex is disassembled in an ATP-dependent reaction catalyzed by NSF, allowing recycling of the SNARE proteins (398).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [398]
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“…due to its function of disassembling the SNARE complex to allow for neurotransmitterrelease and tiestovesicle fusion,including those responsible for bringing additional neurotransmitter receptors to the cell surface (Tolar and Pallanck 1998; Littleton et al. 2001; Yang et al. 2024).”
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Metadata
- Authors
- Littleton, J. T., Barnard, R. J. O., Titus, S. A., Slind, J., Chapman, E. R., & Ganetzky, B.
- Affiliations
- University of Wisconsin–Madison (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-10-02
- Volume
- 98
- Issue
- 21
- Pages
- 12233-12238
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC59797
- OpenAlex
- W2050959850
- Semantic Scholar
- 3803066e22350667cb97543a655caa7de6fa97c4
- Cited by
- 140
- References
- 43
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 6 · 2015: 11 · 2014: 7 · 2012: 4
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm043100-07, NS40296)
- National Institute of General Medical Sciences (R01GM056827, GM56827-01, GM43100)
- National Institute of Neurological Disorders and Stroke (NS15390, R01NS040296, NS40296-01, R01NS015390)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- NSF, SNARE complex disassembly, synaptic vesicle fusion, synaptic vesicle recycling, Pará, shibire, neurotransmission, exocytosis, endocytosis, reserve pool, Drosophila
- MeSH terms
- Alleles, Animals, Carrier Proteins, Drosophila melanogaster, Female, Male, Membrane Fusion, Membrane Proteins, Synaptic Vesicles, Mutagenesis, Vesicular Transport Proteins, SNARE Proteins, N-Ethylmaleimide-Sensitive Proteins
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