HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. - Wikidata - awgldk - TriplyDB

HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.

HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.

http://www.wikidata.org/entity/Q42801354

about

Structural basis of Vps33A recruitment to the human HOPS complex by Vps16 UVRAG is required for virus entry through combinatorial interaction with the class C-Vps complex and SNAREs Coat/Tether Interactions-Exception or Rule?Exorcising the exocyst complex Function and regulation of the endosomal fusion and fission machineries Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.Functional separation of endosomal fusion factors and the class C core vacuole/endosome tethering (CORVET) complex in endosome biogenesis Phosphorylation of the effector complex HOPS by the vacuolar kinase Yck3p confers Rab nucleotide specificity for vacuole docking and fusion.Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex.SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation A lipid-anchored SNARE supports membrane fusion Rab7 and Arl8 GTPases are necessary for lysosome tubulation in macrophages.Importance of the N-terminal domain of the Qb-SNARE Vti1p for different membrane transport steps in the yeast endosomal system.Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.A HOPS protein, CmVps39, is required for vacuolar morphology, autophagy, growth, conidiogenesis and mycoparasitic functions of Coniothyrium minitans.Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes.Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor.Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.Rab GTPases regulating receptor trafficking at the late endosome-lysosome membranes.CAPS and Munc13: CATCHRs that SNARE Vesicles Functional homologies in vesicle tethering.Autophagy in the test tube: In vitro reconstitution of aspects of autophagosome biogenesis.Chaperoning SNARE assembly and disassembly Phosphoinositide-binding proteins in autophagy.Phagocytosis: Hungry, Hungry Cells.A HOPS Protein, MoVps41, Is Crucially Important for Vacuolar Morphogenesis, Vegetative Growth, Reproduction and Virulence in Magnaporthe oryzae.Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes.The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.Rab GTPases and tethering in the yeast endocytic pathway.Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion.Saccharomyces cerevisiae Env7 is a novel serine/threonine kinase 16-related protein kinase and negatively regulates organelle fusion at the lysosomal vacuole.A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion.

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P2860

HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.

http://www.wikidata.org/entity/Q42801354

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

HOPS drives vacuole fusion by ...... domain via two distinct sites.

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HOPS drives vacuole fusion by ...... domain via two distinct sites.

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type

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HOPS drives vacuole fusion by ...... domain via two distinct sites.

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HOPS drives vacuole fusion by ...... domain via two distinct sites.

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prefLabel

HOPS drives vacuole fusion by ...... domain via two distinct sites.

@en

HOPS drives vacuole fusion by ...... domain via two distinct sites.

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P356

MBC.E11-02-0104

P1433

Molecular Biology of the Cell

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HOPS drives vacuole fusion by ...... domain via two distinct sites.

@en

P2093

Christian Ungermann

http://www.w3.org/2001/XMLSchema#string

Lukas Krämer

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P2860

The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8.

Membrane fusion: grappling with SNARE and SM proteins

Vam3p structure reveals conserved and divergent properties of syntaxins

Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.

A Structure-Based Mechanism for Vesicle Capture by the Multisubunit Tethering Complex Dsl1

Defined subunit arrangement and rab interactions are required for functionality of the HOPS tethering complex.

Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones

HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion

The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes.

Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

P304

2601-2611

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scholarly article

P356

10.1091/MBC.E11-02-0104

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14

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22

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P577

2011-05-25T00:00:00Z

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21613544

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3135484

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