The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.
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The diversity of calcium sensor proteins in the regulation of neuronal functionDynamic Ca2+-dependent stimulation of vesicle fusion by membrane-anchored synaptotagmin 1Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosisDynamic binding mode of a Synaptotagmin-1-SNARE complex in solutionStructural and mutational analysis of functional differentiation between synaptotagmins-1 and -7Molecular Machines Regulating the Release Probability of Synaptic Vesicles at the Active ZoneMolecular machines governing exocytosis of synaptic vesiclesA Chemical Controller of SNARE-Driven Membrane Fusion That Primes Vesicles for Ca(2+)-Triggered Millisecond ExocytosisPhosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitmentStructural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complexCis- and trans-membrane interactions of synaptotagmin-1Dipeptidyl peptidase-like protein 6 is required for normal electrophysiological properties of cerebellar granule cellsReconstituting SNARE-mediated membrane fusion at the single liposome level.Variable cooperativity in SNARE-mediated membrane fusion.Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion.Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserinePhosphatidylinositol 4,5-bisphosphate alters synaptotagmin 1 membrane docking and drives opposing bilayers closer together.Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridgingThe calcium-dependent and calcium-independent membrane binding of synaptotagmin 1: two modes of C2B binding.Tomosyn inhibits synaptotagmin-1-mediated step of Ca2+-dependent neurotransmitter release through its N-terminal WD40 repeats.Re-examining how complexin inhibits neurotransmitter release.Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assaySynaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.Membrane bridging and hemifusion by denaturated Munc18.Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex.Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion.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 formationBinding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity.The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening.Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion.Molecular underpinnings of synaptic vesicle pool heterogeneity.Enlightening molecular mechanisms through study of protein interactionsPhosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity.Synaptotagmin-1 C2B domain interacts simultaneously with SNAREs and membranes to promote membrane fusion.Location matters: synaptotagmin helps place vesicles near calcium channels.Functional synergy between the Munc13 C-terminal C1 and C2 domains.Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release.
P2860
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P2860
The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.
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
The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.
@en
type
label
The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.
@en
prefLabel
The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.
@en
P2860
P50
P356
P1476
The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function
@en
P2093
P2860
P2888
P304
P356
10.1038/NSMB.1508
P577
2008-10-26T00:00:00Z