Vam3p structure reveals conserved and divergent properties of syntaxins
about
How Tlg2p/syntaxin 16 'snares' Vps45Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homologConvergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteinsrsly1 binding to syntaxin 5 is required for endoplasmic reticulum-to-Golgi transport but does not promote SNARE motif accessibilityCrystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminusMunc18-1 binding to the neuronal SNARE complex controls synaptic vesicle primingCrystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tardaStructural basis for the Golgi membrane recruitment of Sly1p by Sed5p.Structure of the GAT domain of human GGA1: A syntaxin amino-terminal domain fold in an endosomal trafficking adaptorThe Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering FactorsCrystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*Dissecting Ent3p: the ENTH domain binds different SNAREs via distinct amino acid residues while the C-terminus is sufficient for retrograde transport from endosomes.The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery.Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperonesPhosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionThe specificity of SNARE-dependent fusion is encoded in the SNARE motif.Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes.Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p.Positive and negative regulation of a SNARE protein by control of intracellular localization.The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assemblyVps-C complexes: gatekeepers of endolysosomal traffic.Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.Crystallization and preliminary X-ray diffraction analysis of Gos1p, a yeast SNARE proteinThe longin SNARE VAMP7/TI-VAMP adopts a closed conformation.Functional analysis of conserved structural elements in yeast syntaxin Vam3p.HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly.At the junction of SNARE and SM protein function.Yeast vacuoles and membrane fusion pathwaysA lipid-anchored SNARE supports membrane fusionA complete set of SNAREs in yeast.Class IA phosphatidylinositol 3-kinase p110α regulates phagosome maturation.Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins.Importance of the N-terminal domain of the Qb-SNARE Vti1p for different membrane transport steps in the yeast endosomal system.Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.Synaptotagmin-1 is an antagonist for Munc18-1 in SNARE zippering.An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system
P2860
Q24534195-A2CBA818-9C5F-415A-802B-F2AEF071621CQ24534776-F5B8D369-0036-48F4-9637-B5838F6FA8D1Q24541277-EED84796-4C5F-40F1-92EC-1E107EB7F9D3Q24619563-76252203-AB5E-4A9C-9524-03B49F243D09Q24800287-DF3FA14C-87E6-4A88-9429-562E0723F742Q26269917-E3FDDDDE-8D6D-4D79-BA63-C518F7F91C07Q27639734-674AE917-34EB-48C4-BAF0-17B2A93BE936Q27639933-D1A7C9BB-53E5-470B-AECC-EC28C0549141Q27640868-835416CF-4B23-4B71-AD05-CD9A7379B71BQ27675057-9D16319B-DDAC-4A8D-8DC3-FFFA73917CA2Q27679019-264EC202-B6FE-41BC-8852-DF33B043D9ACQ27930021-67709D6C-45FF-4A17-921F-1E72517BF00FQ27931175-40C307E4-A951-44BE-B4C1-D59E1CEF4FB8Q27931637-9CD8A392-DB0F-4600-93A6-DA93732B75A6Q27931924-8463F64A-84D3-4508-8265-2479BDCC725AQ27932181-44D0F99D-8757-4154-9A45-127425EB1EA6Q27932523-DA2D56B0-4775-4CE7-B4AC-E7930ED95A39Q27933138-25185CCD-ABDD-4ADC-9A12-BB21D1F0599FQ27935373-63726357-2D0A-4C26-B92F-D530CAF95149Q27938882-7435AB8F-67F8-4370-BDFE-51836727A9CDQ27940130-E50212FB-1E58-4287-8C03-0DADD8472551Q27940373-14521CAC-F632-43E9-9FCE-687BC55BE9FAQ28214428-FFE3798B-A25B-4525-B87C-F8DE5E7FDFCFQ33595195-7C050F82-85B6-4732-A213-FA71B4CA83CDQ33841847-AD743ACF-90F1-4ADC-BD43-3043A32B028DQ33872879-21F86719-FA7C-4877-A8AE-180FE206F7CBQ33885354-D61CD560-6CC1-4279-A7A8-9FA38FEFB166Q33946404-C75F3E00-0C96-42E7-A1F3-CE23540DA24DQ33948566-87CE249E-5C1B-4E08-B672-C448BB48F115Q34073357-E845A338-C64D-41BA-A869-716DC6FFF231Q34086175-147824DC-B373-4C93-8286-9B1615DABE45Q34223018-085B07E9-04AF-404F-AF52-873A2B1856BEQ34283635-19A4175B-12BD-43B8-B14C-827665755D87Q34395900-FADCC690-8E00-446A-A8DB-E983B5F301B4Q34630628-34F26446-1C73-48C7-A4E9-073909974672Q34776538-9C8B1280-C720-4FDC-ABB9-4069A6F2862EQ34788804-2767B6D8-B23A-4A41-AE40-8F6DE95D09BAQ34960727-F349DBE6-E415-4590-ABFA-FEB1686BA620Q35451381-A8F8C1C9-2C1E-4457-A759-50AD357C62E7Q35949003-39D92A4D-E8F0-49B0-B6E8-34D613711874
P2860
Vam3p structure reveals conserved and divergent properties of syntaxins
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Vam3p structure reveals conserved and divergent properties of syntaxins
@ast
Vam3p structure reveals conserved and divergent properties of syntaxins
@en
Vam3p structure reveals conserved and divergent properties of syntaxins
@nl
type
label
Vam3p structure reveals conserved and divergent properties of syntaxins
@ast
Vam3p structure reveals conserved and divergent properties of syntaxins
@en
Vam3p structure reveals conserved and divergent properties of syntaxins
@nl
prefLabel
Vam3p structure reveals conserved and divergent properties of syntaxins
@ast
Vam3p structure reveals conserved and divergent properties of syntaxins
@en
Vam3p structure reveals conserved and divergent properties of syntaxins
@nl
P2093
P356
P1476
Vam3p structure reveals conserved and divergent properties of syntaxins
@en
P2093
P2888
P304
P356
10.1038/85012
P577
2001-03-01T00:00:00Z
P5875
P6179
1034336385