N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
about
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.A distinct tethering step is vital for vacuole membrane fusion.Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.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.Munc18a clusters SNARE-bearing liposomes prior to trans-SNARE zippering.
P2860
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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name
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@ast
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@en
type
label
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@ast
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@en
prefLabel
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@ast
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@en
P2860
P356
P1476
N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
@en
P2093
William T Wickner
P2860
P304
17936-17941
P356
10.1073/PNAS.1216201109
P407
P50
P577
2012-10-15T00:00:00Z