Snares and munc18 in synaptic vesicle fusion

@article{Rizo2002SnaresAM,
  title={Snares and munc18 in synaptic vesicle fusion},
  author={Josep Rizo and Thomas C. S{\"u}dhof},
  journal={Nature Reviews Neuroscience},
  year={2002},
  volume={3},
  pages={641-653}
}
The release of neurotransmitters by Ca2+-triggered synaptic vesicle exocytosis is an exquisitely regulated process that is fundamental for interneuronal communication. This process involves several steps and is controlled by a protein machinery that must prevent release before Ca2+ entry into presynaptic terminals, and yet must rapidly induce release on Ca2+ influx. Extensive studies of the components of this machinery have indicated that SNAREs and Munc18-1 are central proteins for membrane… Expand
The molecular machinery of synaptic vesicle exocytosis
  • L. Li, L. Chin
  • Chemistry, Medicine
  • Cellular and Molecular Life Sciences CMLS
  • 2003
TLDR
A review of present knowledge about the molecular mechanisms by which components mediate and/or regulate synaptic vesicle exocytosis uses a set of unique components to meet the special needs of fast Ca2+-triggered neurotransmitter release. Expand
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  • Biology, Medicine
  • Annals of the New York Academy of Sciences
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TLDR
A brief overview is given about the current state of knowledge, focusing on SNAREs involved in neuronal exocytosis, and major progress has been made in unraveling their molecular mechanism. Expand
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TLDR
Understanding the functions of these proteins will be crucial to reach a faithful description of the mechanisms of membrane fusion and neurotransmitter release and has emphasized the essential nature of other proteins for exocytosis. Expand
Munc18-dependent regulation of synaptic vesicle exocytosis by syntaxin-1A in hippocampal neurons
TLDR
It is shown here that overexpression of syntaxin-1A inhibited exocytosis, in a manner that could be rescued by either elevating or reducing external calcium, or increasing action potential firing frequency, suggesting that syntaxin can control the frequency-response characteristics of the presynaptic fusion machinery. Expand
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TLDR
A fundamental role is demonstrated of the SM protein: to act as a stimulatory subunit of its cognate SNARE fusion machinery, enhancing fusion specificity in a reconstituted system. Expand
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TLDR
This chapter reviews the current understanding of the roles played by three SNARE interacting proteins: UNC-13, TOM-1(tomosyn) and UNC-18(Munc18), and discusses studies from both invertebrate and vertebrate model systems. Expand
Regulation of SNARE fusion machinery by fatty acids
TLDR
This analysis highlights the fact that lipids are not a passive platform in vesicle fusion but intimately regulate SNARE function, and direct lipid modification of SNARE fusion proteins and their regulation by fatty acids following phospholipase action are discussed here in detail. Expand
Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis*♦
TLDR
The crystal structure of this core tomosyn SNARE complex is presented, which consists of a four-helical bundle very similar to that of theSNARE complex containing synaptobrevin, indicating that both SNARE complexes represent end products. Expand
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