ArticleThe Journal of cell biology1995
The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
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Who cites it
94 citing papers in PubMed, 337 citations in OpenAlex.
- Botulinum neurotoxin A modulates the axonal release of pathological tau in hippocampal neurons.Toxicon : official journal of the International Society on Toxinology · 2023Article
- Collagen IV-β1-Integrin Influences INS-1 Cell Insulin SecretionFrontiers in cell and developmental biology · 2022Article
- The Urothelium: Life in a Liquid Environment.Physiological reviews · 2020Review
- Simultaneous Release of Multiple Vesicles from Rods Involves Synaptic Ribbons and Syntaxin 3B.Biophysical journal · 2020Article
- Cerebrospinal fluid synaptosomal-associated protein 25 is a key player in synaptic degeneration in mild cognitive impairment and Alzheimer's disease.Alzheimer's research & therapy · 2018Article
- Syntaxins on granules promote docking of granules via interactions with munc18.Scientific reports · 2018Article
- Nitrosative Stress, Hypernitrosylation, and Autoimmune Responses to Nitrosylated Proteins: New Pathways in Neuroprogressive Disorders Including Depression and Chronic Fatigue Syndrome.Molecular neurobiology · 2017Review
- PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter Release Machinery.Cell reports · 2016Article
- Architecture of the Synaptophysin/Synaptobrevin Complex: Structural Evidence for an Entropic Clustering Function at the Synapse.Scientific reports · 2015Article
- Synaptic vesicle recycling: steps and principles.The EMBO journal · 2014Review
- Expression of synaptosomal-associated protein-25 in the rat brain after subarachnoid hemorrhage.Neural regeneration research · 2013Article
- The sphingolipid psychosine inhibits fast axonal transport in Krabbe disease by activation of GSK3β and deregulation of molecular motors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Article
- Synaptic vesicle capture by CaV2.2 calcium channels.Frontiers in cellular neuroscience · 2013Article
- SNARE requirements en route to exocytosis: from many to few.Journal of molecular neuroscience : MN · 2012Review
- Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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- SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion.The Journal of cell biology · 2010Article
- Inhibition of botulinum neurotoxin a toxic action in vivo by synthetic synaptosome- and blocking antibody-binding regions.The protein journal · 2010Article
- Evidence that vesicles undergo compound fusion on the synaptic ribbon.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
34 more citing papers are in PubMed but not listed here.
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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
Syntaxin 1 and synaptosome-associated protein of 25 kD (SNAP-25) are neuronal plasmalemma proteins that appear to be essential for exocytosis of synaptic vesicles (SVs). Both proteins form a complex with synaptobrevin, an intrinsic membrane protein of SVs. This binding is thought to be responsible for vesicle docking and apparently precedes membrane fusion. According to the current concept, syntaxin 1 and SNAP-25 are members of larger protein families, collectively designated as target-SNAP receptors (t-SNAREs), whose specific localization to subcellular membranes define where transport vesicles bind and fuse. Here we demonstrate that major pools of syntaxin 1 and SNAP-25 recycle with SVs. Both proteins cofractionate with SVs and clathrin-coated vesicles upon subcellular fractionation. Using recombinant proteins as standards for quantitation, we found that syntaxin 1 and SNAP-25 each comprise approximately 3% of the total protein in highly purified SVs. Thus, both proteins are significant components of SVs although less abundant than synaptobrevin (8.7% of the total protein). Immunoisolation of vesicles using synaptophysin and syntaxin specific antibodies revealed that most SVs contain syntaxin 1. The widespread distribution of both syntaxin 1 and SNAP-25 on SVs was further confirmed by immunogold electron microscopy. Botulinum neurotoxin C1, a toxin that blocks exocytosis by proteolyzing syntaxin 1, preferentially cleaves vesicular syntaxin 1. We conclude that t-SNAREs participate in SV recycling in what may be functionally distinct forms.
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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.