Synaptotagmin: A Ca2+ sensor that triggers exocytosis?

@article{Chapman2002SynaptotagminAC,
  title={Synaptotagmin: A Ca2+ sensor that triggers exocytosis?},
  author={E. Chapman},
  journal={Nature Reviews Molecular Cell Biology},
  year={2002},
  volume={3},
  pages={498-508}
}
  • E. Chapman
  • Published 2002
  • Chemistry, Medicine
  • Nature Reviews Molecular Cell Biology
It has been fifty years since the discovery that Ca2+ triggers the rapid exocytosis of neurotransmitters from neurons. One of the proteins that has a crucial role in this secretion event is synaptotagmin I, an abundant constituent of synaptic vesicles that binds Ca2+ ions through two C2 domains. These properties prompted the idea that synaptotagmin I might function as a Ca2+-sensor that triggers neurotransmitter release. So does synaptotagmin trigger exocytosis in a Ca2+-dependent manner, and… Expand
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  • 2003
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TLDR
A point mutation in synaptotagmin I is studied that causes a twofold decrease in overall Ca2+ affinity without inducing structural or conformational changes and participates in triggering neurotransmitter release at the synapse. Expand
Kinetics of Synaptotagmin Responses to Ca2+ and Assembly with the Core SNARE Complex onto Membranes
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It is reported that synaptotagmin is "tuned" to sense Ca2+ concentrations that trigger neuronal exocytosis and readily satisfies the kinetic constraints of synaptic vesicle membrane fusion. Expand
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It is reported here that synaptotagmin, a highly conserved synaptic vesicle protein, binds calcium at physiological concentrations in a complex with negatively charged phospholipids, and this binding is specific for calcium and involves the cytoplasmic domain of synaptoagmin. Expand
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It is shown that Complexins, stoichiometric components of the exocytotic core complex, are important regulators of transmitter release at a step immediately preceding vesicle fusion. Expand
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TLDR
The data are consistent with these peptides competitively blocking release after synaptic vesicle docking and indicate that Ca2+ probably initiates neurotransmitter release by regulating the interaction of synaptotagmin with an acceptor protein. Expand
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TLDR
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Findings suggest that synaptotagmin may play a role in the docking of synaptic vesicles at presynap- tic release sites and promotes exocytotic fusion upon local elevation of cytosolic Caw. Expand
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TLDR
The data suggest that Ca2+ triggers S25-C binding to a low-affinity site, initiating trans-complex formation, and pairing of SNARE proteins on apposing membranes leads to bilayer fusion and results in a high-Affinity cis-SNARE complex. Expand
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