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Ca2+-Triggered Synaptic Vesicle Fusion Initiated by Release of Inhibition.
Brunger, Axel T; Leitz, Jeremy; Zhou, Qiangjun; Choi, Ucheor B; Lai, Ying.
Affiliation
  • Brunger AT; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA; Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Department of Structural Biology, Stanford University, Stanford, CA, USA; Department of Photon Science, Stanford Univers
  • Leitz J; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA; Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Department of Structural Biology, Stanford University, Stanford, CA, USA; Department of Photon Science, Stanford Univers
  • Zhou Q; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA; Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Department of Structural Biology, Stanford University, Stanford, CA, USA; Department of Photon Science, Stanford Univers
  • Choi UB; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA; Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Department of Structural Biology, Stanford University, Stanford, CA, USA; Department of Photon Science, Stanford Univers
  • Lai Y; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA; Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA, USA; Department of Structural Biology, Stanford University, Stanford, CA, USA; Department of Photon Science, Stanford Univers
Trends Cell Biol ; 28(8): 631-645, 2018 08.
Article in En | MEDLINE | ID: mdl-29706534
Recent structural and functional studies of the synaptic vesicle fusion machinery suggest an inhibited tripartite complex consisting of neuronal soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs), synaptotagmin, and complexin prior to Ca2+-triggered synaptic vesicle fusion. We speculate that Ca2+-triggered fusion commences with the release of inhibition by Ca2+ binding to synaptotagmin C2 domains. Subsequently, fusion is assisted by SNARE complex zippering and by active membrane remodeling properties of synaptotagmin. This additional, inhibitory role of synaptotagmin may be a general principle since other recent studies suggest that Ca2+ binding to extended synaptotagmin C2 domains enables lipid transport by releasing an inhibited state of the system, and that Munc13 may nominally be in an inhibited state, which is released upon Ca2+ binding to one of its C2 domains.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Synaptic Vesicles / Calcium Limits: Animals / Humans Language: En Journal: Trends Cell Biol Year: 2018 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Synaptic Vesicles / Calcium Limits: Animals / Humans Language: En Journal: Trends Cell Biol Year: 2018 Document type: Article