Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo
about
The structure and function of 'active zone material' at synapsesA manual collection of Syt, Esyt, Rph3a, Rph3al, Doc2, and Dblc2 genes from 46 metazoan genomes--an open access resource for neuroscience and evolutionary biology.Detection of highly curved membrane surfaces using a cyclic peptide derived from synaptotagmin-I.Protein determinants of SNARE-mediated lipid mixing.Regulation of synaptic vesicle docking by different classes of macromolecules in active zone materialCalcium sensitive ring-like oligomers formed by synaptotagminMembrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo.The synaptotagmin juxtamembrane domain is involved in neuroexocytosis.Sequestration of phosphoinositides by mutated MARCKS effector domain inhibits stimulated Ca(2+) mobilization and degranulation in mast cells.Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.Mechanism for calcium ion sensing by the C2A domain of synaptotagmin ICalcium binding by synaptotagmin's C2A domain is an essential element of the electrostatic switch that triggers synchronous synaptic transmission.Different states of synaptotagmin regulate evoked versus spontaneous release.Genetic analysis of synaptotagmin C2 domain specificity in regulating spontaneous and evoked neurotransmitter release.Conformational dynamics of calcium-triggered activation of fusion by synaptotagmin.Phosphatidylserine regulation of Ca2+-triggered exocytosis and fusion pores in PC12 cells.Evidence that electrostatic interactions between vesicle-associated membrane protein 2 and acidic phospholipids may modulate the fusion of transport vesicles with the plasma membraneSphingosine derivatives inhibit cell signaling by electrostatically neutralizing polyphosphoinositides at the plasma membrane.Sr2+ has low efficiency in regulating spontaneous release at the Calyx of Held synapses.
P2860
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P2860
Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
name
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@ast
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@en
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@nl
type
label
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@ast
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@en
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@nl
prefLabel
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@ast
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@en
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@nl
P2093
P2860
P1476
Ca2+-dependent, phospholipid-b ...... ion-secretion coupling in vivo
@en
P2093
Amelia R Striegel
Brie E Paddock
Edwin R Chapman
Noreen E Reist
P2860
P304
P356
10.1523/JNEUROSCI.0197-08.2008
P407
P577
2008-07-01T00:00:00Z