Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
about
GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assemblyTRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion.Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-localized rab proteins and rab-Guanine nucleotide dissociation inhibitorTRAPP stably associates with the Golgi and is required for vesicle dockingHigh-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle dockingThe membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function.mBet3p is required for homotypic COPII vesicle tethering in mammalian cells.Sec34p, 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 fragmentsTethering membrane fusion: common and different players in myoblasts and at the synapseYeast 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 ERThe yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi trafficInitial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteinsRetrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function.The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation.Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranesSequential action of two GTPases to promote vacuole docking and fusionReconstitution of retrograde transport from the Golgi to the ER in vitro.Erv41p and Erv46p: new components of COPII vesicles involved in transport between the ER and Golgi complex.A Rab requirement is not bypassed in SLY1-20 suppression.Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function.A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport.Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex.Function of a plant stress-induced gene, HVA22. Synthetic enhancement screen with its yeast homolog reveals its role in vesicular traffic.Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway.A role for Yip1p in COPII vesicle biogenesis.Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum.A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion.Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartmentsOn and off membrane dynamics of the endoplasmic reticulum-golgi tethering factor p115 in vivoRequirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiaeThe redox sensor TXNL1 plays a regulatory role in fluid phase endocytosis.The complexity of vesicle transport factors in plants examined by orthology search.Transport-vesicle targeting: tethers before SNAREs.ER-Golgi transport defects are associated with mutations in the Sed5p-binding domain of the COPII coat subunit, Sec24pErv14p directs a transmembrane secretory protein into COPII-coated transport vesicles.
P2860
Q22253422-BCEEE7DD-9675-4F5A-BB9E-F81DF97D62D6Q24302367-F3069B81-7960-46B3-945E-AEE7606C2800Q24533229-559C2498-BCE6-49E6-A049-DFDC3FB674D2Q24544621-81328F9C-147C-4210-8313-5BDD7B03EA31Q24600972-AFDB85FA-FEA0-4EE7-9E41-FE6DBA2E43A0Q24658241-472567C3-928E-41B3-9352-DCD5FFDC856BQ24682925-835F8CB8-BEB3-4EEB-8FB7-DD85144B62E9Q24683056-E6568E8F-3728-47FA-A318-67D7BE8CA026Q24683291-145750FE-D003-4BFD-9ED6-177FA35E411DQ24685922-BD6497C2-7FD5-4C00-AC32-7EBB6DF9BE5EQ27023254-03857B1C-49BF-4F2D-9ABA-2A25D543EF66Q27929829-57511F9D-D26A-4869-80F8-E7805BD9EB82Q27929913-A71CF2B9-AB39-48FD-8335-11A753CA14E8Q27930772-FB1021FF-BCCE-4378-82C7-8B35DEA121B3Q27930897-BB5F5760-64D7-4E3A-8E5C-2248EE655424Q27931738-4017C59A-3F86-42BE-9914-B9E9F7CE7703Q27932292-F147CF3B-6319-448C-A8D5-D8902619E9F9Q27932451-DDF3173A-1212-418B-BAD1-119BAB483240Q27933688-0BA4C2E0-D10D-4B53-A0A9-34A69636F8E4Q27933882-8BD7FA12-1A1C-4EAC-A7B6-4022527B2CDCQ27934087-18715690-4E7C-4AEC-A8F2-DE3FCA08AE78Q27934707-E0C0B15A-A7DE-4F8B-8DDF-4BEDCA48D2D5Q27935403-9B34215B-4EB3-4D3B-8747-A831370D8FD0Q27935411-A5463BA8-E8C9-4C9F-8ED7-93A0274F75C5Q27935701-095B68D4-0EAB-48F4-AF6D-8F8E70BB6C2BQ27936138-B699A7C1-A76F-48E5-9836-74301C1F6DA1Q27936628-D081F65F-CFD0-462A-8E8E-218D0948B3CCQ27936694-CF8057AB-0EBA-4E4C-A38E-C9080DFB7ED8Q27939417-FB4E7ECC-3487-4516-AEBD-621A63CF3C4BQ27939812-11478D61-34B4-401F-AA8D-FC0846A7214BQ27939943-C1FC6634-E653-4BB4-BF73-A5B8D9A570B4Q27940079-67703BEA-4762-4CD8-850A-5DD8CB2662DAQ30432882-E36D3677-D93F-41AC-BDD5-0666F7BE016BQ30446220-E2F57226-383A-46FA-85B3-F0CEFCBF25C8Q30494268-2547D425-8AD5-46D4-A2FE-A220151013C9Q33305213-29372B8F-130B-4997-AA50-5DA235EDCC70Q33638393-4C0EF04F-0352-4BB4-972B-D1D15A74BB82Q33772639-D3AC92AA-2292-45FA-8CF3-6F59B6C2CED8Q33911136-9D9675DA-AFD2-4A7B-B22B-AFFEC7C7A40EQ34011746-BDE6D675-00F9-41DE-AFF0-F5B98444ACC4
P2860
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@ast
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@en
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins.
@nl
type
label
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@ast
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@en
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins.
@nl
altLabel
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@en
prefLabel
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@ast
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@en
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins.
@nl
P2860
P3181
P356
P1476
Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.139.5.1097
P407
P577
1997-12-01T00:00:00Z