Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
about
Structural basis of Vps33A recruitment to the human HOPS complex by Vps16Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomesRecruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and AutophagosomesThe HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17Coat/Tether Interactions-Exception or Rule?The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex RegulationMembrane Tethering Complexes in the Endosomal SystemBridging the Gap between Glycosylation and Vesicle TrafficFunction and regulation of the endosomal fusion and fission machineriesCrystal 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 ComplexesThe 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.The HOPS/Class C Vps Complex Tethers High-Curvature Membranes via a Direct Protein-Membrane Interaction.Mutation in VPS33A affects metabolism of glycosaminoglycans: a new type of mucopolysaccharidosis with severe systemic symptomsThe HOPS/class C Vps complex tethers membranes by binding to one Rab GTPase in each apposed membrane.α-granule biogenesis: from disease to discovery.SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a block in endosome maturation in Caenorhabditis elegans.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.Characterization of the Mammalian CORVET and HOPS Complexes and Their Modular Restructuring for Endosome Specificity.Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis.The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes.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.Interaction of the HOPS complex with Syntaxin 17 mediates autophagosome clearance in Drosophila.CAPS and Munc13: CATCHRs that SNARE VesiclesFunctional homologies in vesicle tethering.Chaperoning SNARE assembly and disassemblySM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity.The life cycle of phagosomes: formation, maturation, and resolution.Phagocytosis: Hungry, Hungry Cells.Defining new SNARE functions: the i-SNARE.The Aspergillus nidulans syntaxin PepA(Pep12) is regulated by two Sec1/Munc-18 proteins to mediate fusion events at early endosomes, late endosomes and vacuoles.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.Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion.A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.A short region upstream of the yeast vacuolar Qa-SNARE heptad-repeats promotes membrane fusion through enhanced SNARE complex assembly.
P2860
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P2860
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
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2012年學術文章
@zh-hant
name
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@ast
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@en
type
label
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@ast
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@en
prefLabel
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@ast
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@en
P2860
P356
P1476
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.
@en
P2093
Alexey J Merz
Braden T Lobingier
P2860
P304
P356
10.1091/MBC.E12-05-0343
P577
2012-10-10T00:00:00Z