A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
about
Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes.Human Vam6p promotes lysosome clustering and fusion in vivoRabring7, a novel Rab7 target protein with a RING finger motifThe Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery.The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation.Sequential action of two GTPases to promote vacuole docking and fusionGenetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6.Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.Inhibition of sodium/proton exchange by a Rab-GTPase-activating protein regulates endosomal traffic in yeast.Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusionVac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusionDNA watermarks: a proof of conceptSec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.Yeast vacuoles and membrane fusion pathwaysTracking of the dynamic localization of the Rab-specific HOPS subunits reveal their distinct interaction with Ypt7 and vacuoles.Rab7 and Arl8 GTPases are necessary for lysosome tubulation in macrophages.Sorting out signals in fly endosomes.Rab proteins and the compartmentalization of the endosomal systemExcess vacuolar SNAREs drive lysis and Rab bypass fusionRegulation of lipid droplet dynamics in Saccharomyces cerevisiae depends on the Rab7-like Ypt7p, HOPS complex and V1-ATPaseInterdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles.Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusionA cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusionReview series: Rab GTPases and membrane identity: causal or inconsequential?Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration.A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.The roles of monomeric GTP-binding proteins in macroautophagy in Saccharomyces cerevisiaeReversible, cooperative reactions of yeast vacuole dockingThe N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusionSteric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.Sequential involvement of p115, SNAREs, and Rab proteins in intra-Golgi protein transport.The EGFR odyssey - from activation to destruction in space and time.SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion.Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p.
P2860
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P2860
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
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2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@ast
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@en
type
label
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@ast
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@en
prefLabel
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@ast
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@en
P2093
P2860
P356
P1476
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
@en
P2093
P2860
P304
P356
10.1073/PNAS.160269997
P407
P577
2000-08-01T00:00:00Z