Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+.
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The diversity of calcium sensor proteins in the regulation of neuronal functionDoc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter releaseComplexins: small but capableMolecular machines governing exocytosis of synaptic vesiclesThe stressed synapse: the impact of stress and glucocorticoids on glutamate transmissionDistinct initial SNARE configurations underlying the diversity of exocytosisA Chemical Controller of SNARE-Driven Membrane Fusion That Primes Vesicles for Ca(2+)-Triggered Millisecond ExocytosisComplexin cross-links prefusion SNAREs into a zigzag arrayThe importance of an asymmetric distribution of acidic lipids for synaptotagmin 1 function as a Ca2+ sensorRat and Drosophila synaptotagmin 4 have opposite effects during SNARE-catalyzed membrane fusionSynaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusionSynaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strengthA manual collection of Syt, Esyt, Rph3a, Rph3al, Doc2, and Dblc2 genes from 46 metazoan genomes--an open access resource for neuroscience and evolutionary biology.In vitro system capable of differentiating fast Ca2+-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter releaseC2-domain mediated nano-cluster formation increases calcium signaling efficiency.Lipid mixing and content release in single-vesicle, SNARE-driven fusion assay with 1-5 ms resolution.Autapses and networks of hippocampal neurons exhibit distinct synaptic transmission phenotypes in the absence of synaptotagmin I.Pulling force generated by interacting SNAREs facilitates membrane hemifusion.Loss of synaptotagmin IV results in a reduction in synaptic vesicles and a distortion of the Golgi structure in cultured hippocampal neuronsInvestigation of SNARE-Mediated Membrane Fusion Mechanism Using Atomic Force Microscopy.Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy.Single-molecule studies of the neuronal SNARE fusion machinery.Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assayLead exposure during synaptogenesis alters vesicular proteins and impairs vesicular release: potential role of NMDA receptor-dependent BDNF signalingSynaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission.Characterization of the lipid binding properties of Otoferlin reveals specific interactions between PI(4,5)P2 and the C2C and C2F domains.Differential regulation of synchronous versus asynchronous neurotransmitter release by the C2 domains of synaptotagmin 1.Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion.Calcium sensitive ring-like oligomers formed by synaptotagminSynaptic mitochondria in synaptic transmission and organization of vesicle pools in health and disease.Membrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo.Spontaneous glutamate release is independent of calcium influx and tonically activated by the calcium-sensing receptor.A sequential vesicle pool model with a single release sensor and a Ca(2+)-dependent priming catalyst effectively explains Ca(2+)-dependent properties of neurosecretion.Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.Mechanism and function of synaptotagmin-mediated membrane apposition.Reluctance to membrane binding enables accessibility of the synaptobrevin SNARE motif for SNARE complex formationTransmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter releaseDoc2 is a Ca2+ sensor required for asynchronous neurotransmitter release.Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion.
P2860
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P2860
Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Synaptotagmin arrests the SNAR ...... ne fusion in response to Ca2+.
@en
type
label
Synaptotagmin arrests the SNAR ...... ne fusion in response to Ca2+.
@en
prefLabel
Synaptotagmin arrests the SNAR ...... ne fusion in response to Ca2+.
@en
P2093
P2860
P356
P1476
Synaptotagmin arrests the SNAR ...... ane fusion in response to Ca2+
@en
P2093
Huisheng Liu
Michael C Chicka
P2860
P2888
P304
P356
10.1038/NSMB.1463
P577
2008-07-11T00:00:00Z