ArticleProceedings of the National Academy of Sciences of the United States of America1994
Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 102 citations in OpenAlex.
- Targeting VAMPs in Aging-Related Diseases: From Mechanisms to Pharmacotherapy.Pharmaceutical research · 2026Review
- Use-Dependent, Untapped Dual Kinase Signaling Localized in Brain Learning Circuitry.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- A Novel High-Potency Tetanus Vaccine.mBio · 2020Article
- Tetanus insensitive VAMP2 differentially restores synaptic and dense core vesicle fusion in tetanus neurotoxin treated neurons.Scientific reports · 2020Article
- Review
- Article
- Spontaneous transmitter release is critical for the induction of long-term and intermediate-term facilitation in Aplysia.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- PTP1B dephosphorylates N-ethylmaleimide-sensitive factor and elicits SNARE complex disassembly during human sperm exocytosis.The Journal of biological chemistry · 2009Article
- Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting.Neurotoxicity research · 2006Review
- Differential regulation of transmitter release by alternatively spliced forms of synaptotagmin I.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Tetanus and botulinum neurotoxins: mechanism of action and therapeutic uses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999Review
- Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP.The Biochemical journal · 1998Article
- The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells.The Journal of cell biology · 1998Article
- The secretion of classical and peptide cotransmitters from a single presynaptic neuron involves a synaptobrevin-like molecule.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
- Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
- Metal substitution of tetanus neurotoxin.The Biochemical journal · 1997Article
- Bacterial protein toxins and cell vesicle trafficking.Experientia · 1996Review
- Molecular characterization of the gene coding for GPRP, a class of proteins rich in glycine and proline interacting with membranes in Arabidopsis thaliana.Plant molecular biology · 1996Article
- VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues.The Journal of cell biology · 1996Article
- Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.Infection and immunity · 1996Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synaptobrevin/vesicle-associated membrane protein (VAMP) and syntaxin are potential vesicle donor and target membrane receptors of a docking complex that requires N-ethylmaleimide-sensitive factor (NSF) and soluble NSF-attachment proteins as soluble factors for vesicle fusion with target membranes. Members of this docking complex are the target of clostridial neurotoxins that act as zinc-dependent proteases. Molecular cloning of the Aplysia californica synaptobrevin cDNA revealed a 180-residue polypeptide (M(r), 19,745) with a central transmembrane region and an atypically large C-terminal intravesicular domain. This polypeptide integrates into membranes at both the co- and posttranslational level, as shown by modification of an artificially introduced N-glycosylation site. The soluble and membrane-anchored forms of synaptobrevin are cleaved by the light chains of the botulinal toxins type D and F and by tetanus toxin involving the peptide bonds Lys49-Ile50, Gln48-Lys49, and Gln66-Phe67, respectively. The active center of teh tetanus toxin light chain was identified by site-specific mutagenesis. His233, His237, Glu234, and Glu270/271 are essential to this proteolytic activity. Modification of histidine residues resulted in loss of zinc binding, whereas a replacement of Glu234 only slightly reduced the zinc content.
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