Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion
about
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 exocytosisComplexin clamps asynchronous release by blocking a secondary Ca(2+) sensor via its accessory α helixStructural and mutational analysis of functional differentiation between synaptotagmins-1 and -7The iTRAPs: Guardians of Synaptic Vesicle Cargo Retrieval During EndocytosisMolecular machines governing exocytosis of synaptic vesiclesDistinct initial SNARE configurations underlying the diversity of exocytosisMembrane curvature at a glanceA Chemical Controller of SNARE-Driven Membrane Fusion That Primes Vesicles for Ca(2+)-Triggered Millisecond ExocytosisLateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains.Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformationCdc42p and Fus2p act together late in yeast cell fusion.The importance of an asymmetric distribution of acidic lipids for synaptotagmin 1 function as a Ca2+ sensorCis- and trans-membrane interactions of synaptotagmin-1Rat and Drosophila synaptotagmin 4 have opposite effects during SNARE-catalyzed membrane fusionThe proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins.Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strengthReconstituting SNARE-mediated membrane fusion at the single liposome level.Regulation of fusion pore closure and compound exocytosis in neuroendocrine PC12 cells by SCAMP1Simulation of fusion-mediated nanoemulsion interactions with model lipid bilayers.Tomosyn inhibits synaptotagmin-1-mediated step of Ca2+-dependent neurotransmitter release through its N-terminal WD40 repeats.Forming giant vesicles with controlled membrane composition, asymmetry, and contents.Detection of highly curved membrane surfaces using a cyclic peptide derived from synaptotagmin-I.Atomic-resolution simulations predict a transition state for vesicle fusion defined by contact of a few lipid tails.Puzzling Out Synaptic Vesicle 2 Family Members Functions.A fast, single-vesicle fusion assay mimics physiological SNARE requirements.Phosphomimetic mutation of cysteine string protein-α increases the rate of regulated exocytosis by modulating fusion pore dynamics in PC12 cells.Membrane bending energy and fusion pore kinetics in Ca(2+)-triggered exocytosisDocking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assayHow could SNARE proteins open a fusion pore?In vivo analysis of conserved C. elegans tomosyn domains.Regulation of exocytosis and fusion pores by synaptotagmin-effector interactions.Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission.Differential regulation of synchronous versus asynchronous neurotransmitter release by the C2 domains of synaptotagmin 1.Synaptotagmin's role in neurotransmitter release likely involves Ca(2+)-induced conformational transition.Solution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion.Calcium sensitive ring-like oligomers formed by synaptotagminMonomeric synucleins generate membrane curvature.
P2860
Q24604134-1B862A6E-8BA3-4FC4-931D-9A9C02877EE8Q24633121-5596DAB0-3634-4867-9924-6EA908349435Q26269821-EB26B2A0-E370-4C7A-A3EC-8B5EA983A066Q26269900-54A61B86-9D2E-4B64-92E8-BD7FF23B0E45Q26269910-98DC693B-5939-46E3-B609-A62B23DB687BQ26768190-45D4E8B1-D1E9-48AD-BFE1-BA252235DA0CQ26849286-77244BB1-86F2-4B25-B165-9F1783737A2DQ26866150-A0F16F8D-DDF7-411D-9876-347539305E0AQ27016570-0B914698-22FF-45A2-BDAD-0223B94E2679Q27336160-2BBAA133-76B4-40E4-9ED7-09F8001B95E3Q27339721-2D463F87-A3BA-415B-879C-92FFEBDA4E44Q27660643-CE276399-8869-4418-8414-385EA94DB825Q27937292-9C86FA69-D353-4845-B33C-34BC227A99B7Q28574821-28E42CF1-1D29-44BC-B772-5E56FCB23130Q28575486-3FEA2BD9-96CE-4808-ABA5-033BC9234591Q28580444-B5090664-97FF-40C1-BB96-DAF57F9E7A80Q30156886-646FDD0C-38E4-4C36-8A78-4B472ADA2158Q30278658-E5B595F4-269E-4ABE-98A7-C7F51533B832Q30299902-A757E5DD-6645-463E-BE3C-A8B05B82171EQ30427201-CD70AD94-BEA6-4FD3-AF81-3230D95792BDQ30459662-C1FFA2E1-3F4D-48B0-BC66-D3A8D082B1B4Q30497679-D89944BB-9AB3-41EE-9654-33362D22265CQ30500985-8A3E07C3-E0F4-4E88-B4D1-7EAF3F51831BQ30525734-FD902912-BF02-4B39-98A5-92362201B863Q33619201-0065B361-8055-4C86-9FD4-3004087A17FEQ33710870-8F74BF2B-1F00-41B3-BF7F-9FFF4020657CQ33734625-91911AC6-6BC1-4E3E-B70A-330845D556F3Q33793296-AE6CA3D1-14AB-403D-8B85-4D89A13864F8Q33880350-B5AB7ACB-E4CF-403F-9B56-B85EB9174D37Q33888728-261DC789-C431-4E8D-8DFE-B768FDA6552AQ33918609-0C7870CD-227C-46C1-899F-69060E67162BQ34056130-FBB232E3-73C1-43E2-A07A-26FE4FF651E9Q34063787-9AFD2DA4-E5DA-4D3B-B8BA-923C87B15C61Q34069969-F6DA3BFE-17FC-4141-8700-8909F51FBD03Q34093007-4D83034C-5508-44B2-9782-11FE383D5BC5Q34144056-05D4EC35-0285-47BD-9A25-35EBC25A990BQ34190825-2F7A7888-DCA5-45FF-8931-17B99F97751CQ34191602-C1998660-90D7-43E6-8AC6-A6BF90ECED68Q34281080-EF00F8EB-7F45-4DC5-9C7A-E9F336C0EA50Q34313934-2BECEACF-5E33-465F-BC08-E99E33F47302
P2860
Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion
description
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2009
@ast
im August 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/08/21)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/08/21)
@nl
наукова стаття, опублікована в серпні 2009
@uk
مقالة علمية (نشرت في 21-8-2009)
@ar
name
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@ast
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@en
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@nl
type
label
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@ast
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@en
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@nl
prefLabel
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@ast
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@en
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@nl
P2860
P50
P3181
P1433
P1476
Synaptotagmin-mediated bending ...... tep in Ca(2+)-regulated fusion
@en
P2093
F Mark Dunning
P2860
P304
P3181
P356
10.1016/J.CELL.2009.05.049
P407
P577
2009-08-01T00:00:00Z