Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay

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Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay is …
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scholarly articleQ13442814

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P356DOI10.1074/JBC.M111.269886
P932PMC publication ID3162418
P698PubMed publication ID21730064

P2093author name stringThomas H Söllner
Jörg Malsam
Jean Michel Krause
Susanne Kreye
Yvette Schollmeier
P2860cites workMunc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranesQ21092770
Regulation of the UNC-18-Caenorhabditis elegans syntaxin complex by UNC-13Q77874508
Membrane fusionQ81623456
The synaptic vesicle cycleQ24297813
Munc18/Syntaxin interaction kinetics control secretory vesicle dynamicsQ24315878
A conformational switch in syntaxin during exocytosis: role of munc18.Q24534308
Membrane fusion: grappling with SNARE and SM proteinsQ24633113
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptideQ24645302
Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle primingQ26269917
Munc18-1 binds directly to the neuronal SNARE complexQ26269949
Structural basis for the Golgi membrane recruitment of Sly1p by Sed5pQ27639933
Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formationQ27666423
Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1AQ27765364
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolutionQ27765619
Munc13-1 is essential for fusion competence of glutamatergic synaptic vesiclesQ27863297
Munc18-1 stabilizes syntaxin 1, but is not essential for syntaxin 1 targeting and SNARE complex formationQ27863336
Dual modes of Munc18-1/SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminusQ27863374
Identification of 23 complementation groups required for post-translational events in the yeast secretory pathwayQ27931724
Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexesQ27932523
The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes.Q27932656
Compartmental specificity of cellular membrane fusion encoded in SNARE proteinsQ27935841
Sec1p binds to SNARE complexes and concentrates at sites of secretionQ27939711
SNAP receptors implicated in vesicle targeting and fusionQ28131653
SNAREpins: minimal machinery for membrane fusionQ28131697
Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complexQ28140447
Snares and Munc18 in synaptic vesicle fusionQ28216761
Molecular anatomy of a trafficking organelleQ28274481
Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motifQ28579136
Munc18-1 promotes large dense-core vesicle dockingQ28587706
SNAREs--engines for membrane fusionQ29547230
Synaptic assembly of the brain in the absence of neurotransmitter secretionQ29618899
Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxinQ29620437
SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranesQ30481470
Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complexQ33797927
SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion.Q34026722
The fusion pores of Ca2+ -triggered exocytosisQ34037133
Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins.Q34092721
Fusion of cells by flipped SNAREsQ34205790
Use of resonance energy transfer to monitor membrane fusionQ34283693
Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis.Q34305380
SNARE proteins and 'membrane rafts'.Q34625388
Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteinsQ34630628
Principles of exocytosis and membrane fusionQ35778275
Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpinsQ36323855
Three SNARE complexes cooperate to mediate membrane fusionQ36538800
Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domainQ36545881
UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxinQ36854983
Munc18-1 in secretion: lonely Munc joins SNARE team and takes control.Q36980038
Munc18a scaffolds SNARE assembly to promote membrane fusionQ36992879
The carboxy-terminal domain of complexin I stimulates liposome fusionQ37077511
Membrane fusion: SNAREs and regulationQ37251858
Interplay between lipids and the proteinaceous membrane fusion machineryQ37274792
Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cellsQ37372099
Defects in synaptic vesicle docking in unc-18 mutantsQ37417567
Rescue of Munc18-1 and -2 double knockdown reveals the essential functions of interaction between Munc18 and closed syntaxin in PC12 cellsQ37448299
Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuolesQ37762546
Munc18-1 as a key regulator of neurosecretionQ37777421
Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundleQ39482880
Munc18-1 prevents the formation of ectopic SNARE complexes in living cellsQ40040679
Munc18-1: sequential interactions with the fusion machinery stimulate vesicle docking and priming.Q40096413
Molecular dissection of the Munc18c/syntaxin4 interaction: implications for regulation of membrane trafficking.Q40245471
Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: prevention by rbSEC1.Q40952260
A role for the syntaxin N-terminus.Q40966553
The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion.Q41081804
nSec1 binds a closed conformation of syntaxin1A.Q41716307
An open form of syntaxin bypasses the requirement for UNC-13 in vesicle primingQ41768196
Functionally and spatially distinct modes of munc18-syntaxin 1 interactionQ41781926
Mechanism of arachidonic acid action on syntaxin-Munc18.Q41821252
ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner.Q41831887
Selective activation of cognate SNAREpins by Sec1/Munc18 proteinsQ42506708
One SNARE complex is sufficient for membrane fusionQ42531466
UNC-13 is required for synaptic vesicle fusion in C. elegansQ43240851
Syntaxin 1A is delivered to the apical and basolateral domains of epithelial cells: the role of munc-18 proteins.Q43760162
Binding of UNC-18 to the N-terminus of syntaxin is essential for neurotransmission in Caenorhabditis elegansQ44590216
Mutations in the Drosophila Rop gene suggest a function in general secretion and synaptic transmissionQ46071055
Arachidonic acid potentiates exocytosis and allows neuronal SNARE complex to interact with Munc18aQ48332407
Anatomy and dynamics of a supramolecular membrane protein cluster.Q50668558
Synaptotagmin-1 Docks Secretory Vesicles to Syntaxin-1/SNAP-25 Acceptor ComplexesQ56992446
N- to C-Terminal SNARE Complex Assembly Promotes Rapid Membrane FusionQ63610158
P4510describes a project that usesImageJQ1659584
P433issue35
P407language of work or nameEnglishQ1860
P304page(s)30582-30590
P577publication date2011-07-05
P1433published inJournal of Biological ChemistryQ867727
P1476titleResolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay
P478volume286