ArticleThe Biochemical journal2001
Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
42 citing papers in PubMed, 94 citations in OpenAlex.
- SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane.Blood · 2007Trial
- Protein lipidation in cardiovascular homeostasis, development, and disease.Clinical science (London, England : 1979) · 2026Review
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- How Botulinum Neurotoxin Light Chain A1 Maintains Stable Association with the Intracellular Neuronal Plasma Membrane.Toxins · 2022Article
- Article
- Vesicle Fusion as a Target Process for the Action of Sphingosine and Its Derived Drugs.International journal of molecular sciences · 2022Review
- A sticky situation: regulation and function of protein palmitoylation with a spotlight on the axon and axon initial segment.Neuronal signaling · 2021Review
- Sarcopenia associates with SNAP-25 SNPs and a miRNAs profile which is modulated by structured rehabilitation treatment.Journal of translational medicine · 2021Article
- Article
- Glutathione contributes to efficient post-Golgi trafficking of incoming HPV16 genome.PloS one · 2019Article
- Emerging evidence for the modulation of exocytosis by signalling lipids.FEBS letters · 2018Review
- Proteomic Analysis of S-Palmitoylated Proteins in Ocular Lens Reveals Palmitoylation of AQP5 and MP20.Investigative ophthalmology & visual science · 2018Article
- Article
- Hypothesis - buttressed rings assemble, clamp, and release SNAREpins for synaptic transmission.FEBS letters · 2017Review
- Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane.eLife · 2017Article
- Reduced SNAP-25 increases PSD-95 mobility and impairs spine morphogenesis.Cell death and differentiation · 2015Article
- Sod1 gene ablation in adult mice leads to physiological changes at the neuromuscular junction similar to changes that occur in old wild-type mice.Free radical biology & medicine · 2015Article
- Termination and initial branch formation of SNAP-25-deficient thalamocortical fibres in heterochronic organotypic co-cultures.The European journal of neuroscience · 2012Article
- SNAP-25 contains non-acylated thiol pairs that can form intrachain disulfide bonds: possible sites for redox modulation of neurotransmission.Cellular and molecular neurobiology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The release of neurotransmitter at a synapse occurs via the regulated fusion of synaptic vesicles with the plasma membrane. The fusion of the two lipid bilayers is mediated by a protein complex that includes the plasma membrane target soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (t-SNAREs), syntaxin 1A and synaptosome-associated protein of 25 kDa (SNAP-25), and the vesicle SNARE (v-SNARE), vesicle-associated membrane protein (VAMP). Whereas syntaxin 1A and VAMP are tethered to the membrane by a C-terminal transmembrane domain, SNAP-25 has been suggested to be anchored to the membrane via four palmitoylated cysteine residues. We demonstrate that the cysteine residues of SNAP-25 are not required for membrane localization when syntaxin 1A is present. Analysis of the 7 S and 20 S complexes formed by mutants that lack cysteine residues demonstrates that the cysteines are required for efficient SNARE complex dissociation. Furthermore, these mutants are unable to support exocytosis, as demonstrated by a PC12 cell secretion assay. We hypothesize that syntaxin 1A serves to direct newly synthesized SNAP-25 through the Golgi transport pathway to the axons and synapses, and that palmitoylation of cysteine residues is not required for targeting, but to optimize interactions required for SNARE complex dissociation.
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What OpenQuestion holds
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.