Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability. - Wikidata - awgldk - TriplyDB

Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability.

Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability.

http://www.wikidata.org/entity/Q36274550

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Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation Exorcising the exocyst complex Regulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activation Structures and mechanisms of vesicle coat components and multisubunit tethering complexes Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes The TRAPP complex: insights into its architecture and function Comparative genomic analysis of multi-subunit tethering complexes demonstrates an ancient pan-eukaryotic complement and sculpting in Apicomplexa Role of Rab GTPases in membrane traffic and cell physiology The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery.Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes.Organization of SNAREs within the Golgi stack Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex.Transport according to GARP: receiving retrograde cargo at the trans-Golgi network.Molecular organization of the COG vesicle tethering complex.The Caenorhabditis elegans GARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology.The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae.The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport.Chlamydia trachomatis hijacks intra-Golgi COG complex-dependent vesicle trafficking pathway.Defects in the COG complex and COG-related trafficking regulators affect neuronal Golgi function.COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity Molecular insights into vesicle tethering at the Golgi by the conserved oligomeric Golgi (COG) complex and the golgin TATA element modulatory factor (TMF)COG complexes form spatial landmarks for distinct SNARE complexes.COG Complex Complexities: Detailed Characterization of a Complete Set of HEK293T Cells Lacking Individual COG Subunits The Golgi puppet master: COG complex at center stage of membrane trafficking interactions.Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs.Role of vesicle tethering factors in the ER-Golgi membrane traffic.Multipronged interaction of the COG complex with intracellular membranes.New links between vesicle coats and Rab-mediated vesicle targeting.How Golgi glycosylation meets and needs trafficking: the case of the COG complex.Structure of Golgi transport proteins.COPII and COPI traffic at the ER-Golgi interface.Retrograde vesicle transport in the Golgi.Re'COG'nition at the Golgi.Secretory protein biogenesis and traffic in the early secretory pathway

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P2860

Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability.

http://www.wikidata.org/entity/Q36274550

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

Interaction of the conserved o ...... Golgi SNARE complex stability.

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Interaction of the conserved o ...... Golgi SNARE complex stability.

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type

label

Interaction of the conserved o ...... Golgi SNARE complex stability.

@ast

Interaction of the conserved o ...... Golgi SNARE complex stability.

@en

prefLabel

Interaction of the conserved o ...... Golgi SNARE complex stability.

@ast

Interaction of the conserved o ...... Golgi SNARE complex stability.

@en

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Interaction of the conserved o ...... Golgi SNARE complex stability.

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P2093

Anna Shestakova

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Elena Suvorova

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Galimat Khaidakova

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Oleksandra Pavliv

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Vladimir Lupashin

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P2860

Purification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transport

Identification of a human orthologue of Sec34p as a component of the cis-Golgi vesicle tethering machinery

The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic

Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function

COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation

Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder

The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins

rsly1 binding to syntaxin 5 is required for endoplasmic reticulum-to-Golgi transport but does not promote SNARE motif accessibility

A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack

High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking

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1179-1192

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10.1083/JCB.200705145

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6

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179

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5761696

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18086915

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2140037

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