Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay.
about
Neurotransmitter release: the last millisecond in the life of a synaptic vesicleSyntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusionReconciling the regulatory role of Munc18 proteins in SNARE-complex assemblySyntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformationSyntaxin binding mechanism and disease-causing mutations in Munc18-2An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly.SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1.The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulationLow-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.Mutant SNAP25B causes myasthenia, cortical hyperexcitability, ataxia, and intellectual disability.Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular CrowdingThe trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosisComparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Munc18-2 and syntaxin 3 control distinct essential steps in mast cell degranulationHOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.CAPS and Munc13: CATCHRs that SNARE VesiclesC2-domain containing calcium sensors in neuroendocrine secretion.The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly.Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly.
P2860
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P2860
Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Resolving the function of dist ...... tituted membrane fusion assay.
@ast
Resolving the function of dist ...... tituted membrane fusion assay.
@en
type
label
Resolving the function of dist ...... tituted membrane fusion assay.
@ast
Resolving the function of dist ...... tituted membrane fusion assay.
@en
prefLabel
Resolving the function of dist ...... tituted membrane fusion assay.
@ast
Resolving the function of dist ...... tituted membrane fusion assay.
@en
P2093
P2860
P356
P1476
Resolving the function of dist ...... tituted membrane fusion assay.
@en
P2093
Jean Michel Krause
Jörg Malsam
Susanne Kreye
Thomas H Söllner
Yvette Schollmeier
P2860
P304
30582-30590
P356
10.1074/JBC.M111.269886
P407
P577
2011-07-05T00:00:00Z