Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
about
Identification and characterization of Iporin as a novel interaction partner for rab1TMF is a golgin that binds Rab6 and influences Golgi morphologyPurification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transportGATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi and exists in a complex with GTC-90 and ldlBpDirect interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairingThe Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1bDistinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity.CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantinGranuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1aGenetic analysis of yeast Yip1p function reveals a requirement for Golgi-localized rab proteins and rab-Guanine nucleotide dissociation inhibitorAccumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosisA novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targetingTRAPP stably associates with the Golgi and is required for vesicle dockingAssembly, organization, and function of the COPII coatSequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35pPhosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragmentsThe mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130Coat/Tether Interactions-Exception or Rule?Exorcising the exocyst complexTethering membrane fusion: common and different players in myoblasts and at the synapseStructural basis for the Golgi membrane recruitment of Sly1p by Sed5p.Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane TetheringYeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ERAn effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes.Ordering the final events in yeast exocytosis.Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs.The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi trafficThe yeast Rab GTPase Ypt1 modulates unfolded protein response dynamics by regulating the stability of HAC1 RNA.SM-protein-controlled ER-associated degradation discriminates between different SNAREs.Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunitToward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteinsAsymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranesVps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late GolgiThree v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiaeVam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.Erv41p and Erv46p: new components of COPII vesicles involved in transport between the ER and Golgi complex.
P2860
Q21284171-78955DAE-B710-4B04-84B9-0AFD73D3D4EBQ21284177-3B4164B5-84F0-48CF-A731-7EAB5AD9C5BBQ22004165-6ADF72CF-8A15-4E22-8786-8D586EA9EE7FQ22253422-67486000-60D9-42BA-AC6B-593D86D1229FQ24293147-6BA96BCD-10C6-4EEA-9C71-5C59E984F4ADQ24338692-BF650C38-2595-4B23-9A01-BCF7BA2E0312Q24522514-B226C748-EC2B-47E5-8C80-74DE1DDB3F3FQ24534126-E2C96382-91D8-4E1B-A68C-342823D3620EQ24537148-56A836E5-481B-44EA-9445-F3024CCC1830Q24537609-DD938396-B543-45C4-98CE-0B576D1D7997Q24544621-1A02D34E-FC3F-4DEC-AECE-52DBFBB76179Q24550107-B77B0165-9EAF-4378-A38B-75FA8176C2F1Q24598323-A3444A56-5F34-41F6-87B0-12EC04FF974BQ24600972-B6451E6B-F957-4D09-8460-F517331EBF24Q24655263-3D3858B5-1C74-489C-A3DA-2D03069F610CQ24673491-E0AC4CA8-5E4A-48C8-B17C-475CAC6C9A2AQ24683291-92D76C82-AF61-4E93-A4B1-88E9F955A779Q24685922-F403D383-C0CA-4AED-B228-F52AFB5C7B56Q24685935-B0076707-C4A0-4626-B6E2-CF65F14C3F56Q26744484-E90CBF6C-24CD-4F50-9B98-D9E2157E651FQ26824772-B0E1E853-4A99-4445-88E1-1E2CE62BDAC5Q27023254-561D6124-AF32-4007-A20A-993AB812234DQ27639933-1289A808-4B29-4630-BA4D-57CC87DD885BQ27655362-F823B275-F790-4EAD-8351-E41F77C33621Q27929829-C696C452-AA46-4A01-8B32-DACC21731ABBQ27929913-8BA822B7-77FB-4CAB-8AB7-8E07E4D652BCQ27930206-261A8084-EFA2-410F-A239-70A1EA89C848Q27930282-3A5B0134-E506-4598-8506-437392D7CF3AQ27930315-EE10868B-6EB7-4383-B412-C4DAE3E7D248Q27930772-249D59C2-A5F1-479E-885D-0E09C0D14DA8Q27932190-BB8862CE-5054-4EA7-9DC6-5C20DE0AA0D7Q27932266-31238513-78FC-4F75-84A3-085A55B62743Q27932312-B54A4588-51CD-4BC3-BD42-72BDB6905813Q27932356-B3D26BF1-A0BE-4B4F-93BF-FF0B90859052Q27932451-024C1171-FA64-409F-9411-B89A712EEAEDQ27932636-A648076D-B503-4E66-90EA-E9F7438B06BBQ27932817-AE00B056-6821-4F9B-BA64-5AC1A694AF20Q27933048-BAB23F0E-EA9B-43D7-A580-B6B92DB59316Q27933694-B0352CDD-218D-4CD7-ACAA-36AC2D140D8DQ27934087-B78D0AE7-1FBC-4B7A-A0E1-C40B864DC1F9
P2860
Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Initial docking of ER-derived ...... independent of SNARE proteins
@ast
Initial docking of ER-derived ...... independent of SNARE proteins
@en
Initial docking of ER-derived ...... independent of SNARE proteins.
@nl
type
label
Initial docking of ER-derived ...... independent of SNARE proteins
@ast
Initial docking of ER-derived ...... independent of SNARE proteins
@en
Initial docking of ER-derived ...... independent of SNARE proteins.
@nl
prefLabel
Initial docking of ER-derived ...... independent of SNARE proteins
@ast
Initial docking of ER-derived ...... independent of SNARE proteins
@en
Initial docking of ER-derived ...... independent of SNARE proteins.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Initial docking of ER-derived ...... independent of SNARE proteins
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/17.8.2156
P407
P577
1998-04-01T00:00:00Z