Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.
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Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter releaseReconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperonesPhosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionHOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusionHOPS proofreads the trans-SNARE complex for yeast vacuole fusionPhosphatidylinositol-4,5-bisphosphate and phospholipase D-generated phosphatidic acid specify SNARE-mediated vesicle fusion for prospore membrane formation.Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion.A lipid-anchored SNARE supports membrane fusionPhosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly.The Gos28 SNARE protein mediates intra-Golgi transport of rhodopsin and is required for photoreceptor survival.Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathwayImportance 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.Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.Impairment of autophagosome-lysosome fusion in the buff mutant mice with the VPS33A(D251E) mutation.The structural and functional implications of linked SNARE motifs in SNAP25The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Mechanics of membrane fusion.The SNARE complex from yeast is partially unstructured on the membrane.Transmembrane protein-free membranes fuse into xenopus nuclear envelope and promote assembly of functional pores.ESCRTs function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteinsA cascade of multiple proteins and lipids catalyzes membrane fusion.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
Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.
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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name
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@ast
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@en
type
label
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@ast
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@en
prefLabel
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@ast
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@en
P2093
P2860
P356
P1433
P1476
Sec18p and Vam7p remodel trans ...... support yeast vacuole fusion.
@en
P2093
Naomi Thorngren
William Wickner
Youngsoo Jun
P2860
P304
P356
10.1038/SJ.EMBOJ.7601915
P407
P577
2007-11-15T00:00:00Z