Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
about
Munc18/Syntaxin interaction kinetics control secretory vesicle dynamics.Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptideMunc18-1 binding to the neuronal SNARE complex controls synaptic vesicle primingMunc18-1 binds directly to the neuronal SNARE complexBridging the Gap between Glycosylation and Vesicle TrafficReconciling the regulatory role of Munc18 proteins in SNARE-complex assemblyTracking individual secretory vesicles during exocytosis reveals an ordered and regulated process.Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*Syntaxin binding mechanism and disease-causing mutations in Munc18-2Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.Yeast Sec1p functions before and after vesicle docking.SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.At the junction of SNARE and SM protein function.Network motif comparison rationalizes Sec1/Munc18-SNARE regulation mechanism in exocytosis.Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins.Hemophagocytic lymphohistiocytosis caused by dominant-negative mutations in STXBP2 that inhibit SNARE-mediated membrane fusion.The GTPase-activating protein Rga1 interacts with Rho3 GTPase and may regulate its function in polarized growth in budding yeast.Trans-SNARE complex assembly and yeast vacuole membrane fusion.Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.Quantitative Proteomic Analysis Reveals Molecular Adaptations in the Hippocampal Synaptic Active Zone of Chronic Mild Stress-Unsusceptible Rats.Synaptic vesicle fusion.The SNARE complex from yeast is partially unstructured on the membrane.The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/SNAP-25.Chaperoning SNARE assembly and disassemblyBinding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle.Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.Septin-containing barriers control the differential inheritance of cytoplasmic elements.A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins.Sec1p and Mso1p C-terminal tails cooperate with the SNAREs and Sec4p in polarized exocytosis.HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.Munc-18-1 regulates the initial release rate of exocytosis.Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins.An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.
P2860
Q24315878-3C199A0F-437A-48E0-B602-983161D6F7ACQ24645302-FE0D0C28-D831-4932-8DF0-5181BC31694BQ26269917-A40205A0-51B5-4AD0-A06B-217E897D774BQ26269949-B0A055C1-49DD-4DB2-B3DF-BDA723D39FF6Q26750822-E38FC8EE-5F62-43BE-B340-276CE71035ECQ26821963-58918FFF-AD4D-4EA6-BAEE-5AE020244FE1Q27310147-E367F01B-56CA-43F9-AE33-FF184C7C8138Q27679019-9663BA35-8804-4959-826D-89D3853D88C4Q27680537-55FBAE89-1E3E-4BF4-A34C-CB2C21B14DA9Q27937182-84FD2F86-88A6-4AB3-967C-48EB586A74BCQ30381017-BB05B595-F1C7-4888-B8CA-40FB2956164AQ33764725-5167B510-A7E7-4A1B-AD7D-1417FEE0EFCAQ34073357-CC11119D-C588-4D63-9829-759FED94D493Q34198065-4346F2D9-8FB0-4AD3-A8DC-DAB0DA37AA8DQ34630628-BF3CC34C-833D-4D09-956A-9E239D049C14Q35153210-57D7413A-EAF3-425C-BDFB-A048A2B60612Q35599051-10006C06-E7CE-4722-8781-F8B44BC15A2CQ35828995-1A29EF4F-F53D-416A-8C56-9FEEE5EF6868Q35932279-E7D7565B-1187-46BC-BA14-FB16ED41CA99Q36433806-B992471A-540A-4371-8BD8-FC79B2F91EBEQ36634050-0EF0F5CE-9A4E-438B-B9BD-A47E10A40DA6Q36844178-CB627C6F-8AC6-4C51-AA56-D55801F486AEQ37069857-26093B9E-43C8-4894-B1BC-EAF7DB56EBCBQ37321091-9D3CF9EE-DCEB-4DDA-86DB-B436AC740704Q38819431-2810A552-0DBB-4016-9ECE-0C00601A69D9Q38865222-BDB7FDDF-4D59-4822-8A17-9E9942291C68Q39482880-64139BBD-3C68-46B8-BB48-30DAB32A9BF9Q40007813-49DBD439-1B1F-4E47-9714-86944DAA548CQ42073173-15D79026-1362-4E13-AFED-48556D008666Q42526016-EF773CD4-5F1F-47A1-8535-1EB66F6A4B45Q42571521-161AB159-3FF3-4888-879F-EFBB4D3A2873Q42801354-C1C13B7E-F37E-4C43-9932-3E192D73334DQ42935665-308DD231-08D2-44ED-9EAE-16EFCE92ED72Q47133346-2C15D315-96CF-4735-A75F-0311C0CB55BDQ48175402-C92970ED-EB6D-4DC4-9F0A-A1F6F236A0FD
P2860
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
description
2006 nî lūn-bûn
@nan
2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@ast
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@en
type
label
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@ast
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@en
prefLabel
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@ast
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@en
P2093
P2860
P356
P1476
Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p.
@en
P2093
Chavela M Carr
Frederick M Hughson
John Togneri
Mary Munson
Yi-Shan Cheng
P2860
P304
17730-17735
P356
10.1073/PNAS.0605448103
P407
P577
2006-11-07T00:00:00Z