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How does synaptotagmin trigger neurotransmitter release?
  • E. Chapman
  • Biology, Medicine
  • Annual review of biochemistry
  • 2 June 2008
Findings obtained from genetically modified neurons and neuroendocrine cells, as well as from reconstituted systems, are summarized to reveal the molecular mechanism by which Ca(2+)-acting on the synaptic vesicle (SV) protein synaptotagmin I (syt)-triggers rapid exocytosis. Expand
SV2 Is the Protein Receptor for Botulinum Neurotoxin A
It is found that BoNT/A enters neurons by binding to the synaptic vesicle protein SV2 (isoforms A, B, and C), and SV2 acts as the protein receptor for Bo NT/A. Expand
Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25
It is demonstrated that BoNT/A acts as a zinc-dependent protease that selectively cleaves SNAP-25, a second component of the putative fusion complex mediating synaptic vesicle exocytosis is targeted by a clostridial neurotoxin. Expand
Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine.
It is concluded that synaptophysin selectively interacts with synaptobrevin in a complex which excludes the t‐SNAP receptors syntaxin I and SNAP‐25, suggesting a role for synaptophysicalin in the control of exocytosis. Expand
PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
It is proposed that syt-PIP2 interactions are involved in exocytosis by facilitating the close apposition of the vesicle and target membrane on rapid time scales in response to Ca2+. Expand
Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC‐1/syntaxin.
It is concluded that HPC‐1/syntaxin, a membrane protein present in axonal and synaptic membranes, is involved in exocytotic membrane fusion. Expand
Synaptotagmin Modulation of Fusion Pore Kinetics in Regulated Exocytosis of Dense-Core Vesicles
In the exocytosis of neurotransmitter, fusion pore opening represents the first instant of fluid contact between the vesicle lumen and extracellular space, and synaptotagmin interacts with fusion pores by associating with a core complex of membrane proteins and/or lipid. Expand
Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons.
It is demonstrated that glycosylated SV2A and SV2B act in conjunction with gangliosides to mediate the entry of BoNT/E into neurons. Expand
Different domains of synaptotagmin control the choice between kiss-and-run and full fusion
Amperometric recordings of catecholamine efflux through individual fusion pores show that Syt regulates the choice between full fusion and kiss-and-run, with Ca2+ binding to the C2A and C2B domains playing an important role in this choice. Expand
Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells
It is reported here that the secretory vesicle proteins, synaptotagmins (syts) I and II, mediate the entry of BoNT/B into PC12 cells and rat diaphragm motor nerve terminals and shown that syt II fragments, in conjunction with gangliosides, neutralized Bo NT/B in intact mice. Expand