Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
about
Identification of a human orthologue of Sec34p as a component of the cis-Golgi vesicle tethering machinerySec34 is implicated in traffic from the endoplasmic reticulum to the Golgi and exists in a complex with GTC-90 and ldlBpCharacterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and functionCOG-7-deficient Human Fibroblasts Exhibit Altered Recycling of Golgi ProteinsDirect interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairingThe COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteinsTRAPP 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 dockingSec34p, 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 fragmentsStructural analysis of conserved oligomeric Golgi complex subunit 2Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteinsGolgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunitVps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late GolgiRetrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport 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.Role of the spindle pole body of yeast in mediating assembly of the prospore membrane during meiosisThe conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy.The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast.The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins.Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex.Subunit architecture of the conserved oligomeric Golgi complexGenetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cellsThe interaction of two tethering factors, p115 and COG complex, is required for Golgi integrityRole of Rab GTPases in membrane traffic and cell physiologyRabs and their effectors: achieving specificity in membrane trafficCOG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.On and off membrane dynamics of the endoplasmic reticulum-golgi tethering factor p115 in vivoPost-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transportTransport-vesicle targeting: tethers before SNAREs.Identification of Sec36p, Sec37p, and Sec38p: components of yeast complex that contains Sec34p and Sec35p.Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes.Munc18c function is required for insulin-stimulated plasma membrane fusion of GLUT4 and insulin-responsive amino peptidase storage vesicles.YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins.Membrane tethering and fusion in the secretory and endocytic pathways.Organization of SNAREs within the Golgi stackThe Drosophila Cog5 homologue is required for cytokinesis, cell elongation, and assembly of specialized Golgi architecture during spermatogenesis.Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II.
P2860
Q24291101-9043A0B3-8EAE-424E-ABB3-3F1DE66948B1Q24293147-F3399140-91A2-4188-9319-C6F43CC3836CQ24296062-16CBAC7E-6436-4B3E-A8DF-8E52DA985BABQ24306195-2F41C5E0-6BF4-4C69-9B89-9FFF8398B479Q24338692-6B97AA44-57ED-43B3-87D2-1B6DF5AFAC83Q24564894-CC4CB81F-9935-4AF6-ABEA-FCD2CD86B708Q24600972-E8D555CD-311C-4E16-A90B-03AA7D2F3148Q24658241-68B6BC1F-41B1-4263-A746-535748621729Q24683291-F193DB53-2730-4E26-9481-236B8F862D81Q24685922-5C761699-ED60-4649-8E8A-A942D77E1DE2Q27645684-AEBF43E5-4CC6-4741-9D08-08571969AB07Q27931624-F6B5F8A9-6A4F-4A97-AA4D-2ECD40E1291EQ27932312-640E8D5D-A64A-413E-B5CB-F46F2369B3B2Q27932636-C4AB1520-ACA0-4EAD-B536-D90041C22A5CQ27932804-C2057973-4F83-453B-9F3E-83741BCD15CAQ27934707-90EC7197-6941-4074-81D3-341E458FC23BQ27935403-0B72A3F9-8E12-4617-B0D5-C55F57BDC007Q27935485-40EA2937-C7D2-43FB-9974-8B681405A856Q27935788-A4FC0260-5E79-4405-B953-CA458EFC7357Q27936358-8DE3F2AC-672B-4CF7-97B8-1AB44C9DF615Q27937701-88DC8DE2-FC70-46D8-93F8-69FB4BFE384BQ27939812-F02C6552-9290-4BE0-8969-16006A728FD8Q27939894-A4E1E15B-D73D-4EC4-B455-C796F96D5D3DQ28261773-FAD4F934-33F1-49C1-8F7D-70B9236F9128Q28264202-A0DAA19C-3645-4D38-8C61-64EB5AB24A4CQ28286629-7B12A9C0-7BB4-4A51-A118-31000501C251Q29616548-24FE15E9-F68F-42CD-A156-3E8B87804A7DQ29619989-51C2336C-C8DD-4D8D-B703-5E1AAD5088E3Q30379553-97059DB3-9D29-4354-AC65-401EA58A15FCQ30446220-F7579EC7-A089-4AE3-BBE4-59D0986FF63AQ33112690-A723815E-5997-4EF9-95D8-BFE849A5DE1DQ33772639-5B44440F-D9A7-42B0-A210-988D9C76267CQ33787817-69427B7E-397E-430E-9D4D-1FCC8C4E9E36Q33854507-C4C60E21-3B7A-42FE-8F0A-398B35AB9661Q33961324-415FBDD0-3650-481B-AA16-46920C573A64Q34134524-CDB247A8-2A50-46C2-92D0-504B983B9FC5Q34156712-963E6998-C381-40E2-97AC-3041E8FAD5D3Q34201603-FCC204D9-D7AD-4177-9045-B2F10A5143D6Q34451188-C66A88D3-A31B-466A-8BBD-8FB306EF96D2Q34574535-4E83E867-C6F3-46CD-8457-D346A07A86BB
P2860
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@ast
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@en
type
label
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@ast
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@en
prefLabel
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@ast
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@en
P2093
P2860
P356
P1476
Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking.
@en
P2093
M G Waters
S M VanRheenen
V V Lupashin
P2860
P304
P356
10.1083/JCB.141.5.1107
P407
P577
1998-06-01T00:00:00Z