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HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
18385512
retrieved
1 December 2016
title
HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
(English)
1 reference
stated in
PubMed
PubMed ID
18385512
retrieved
1 December 2016
main subject
cell biology
0 references
Tethering complex ATP-binding subunit VPS33 YLR396C
1 reference
stated in
GOA release 2020-03-11
Vam6p YDL077C
1 reference
stated in
GOA release 2020-03-11
Tethering complex subunit PEP3 YLR148W
1 reference
stated in
GOA release 2020-03-11
Vps41p YDR080W
1 reference
stated in
GOA release 2020-03-11
Tethering complex subunit VPS16 YPL045W
1 reference
stated in
GOA release 2020-03-11
Tethering complex subunit PEP5 YMR231W
1 reference
stated in
GOA release 2020-03-11
vacuole
1 reference
based on heuristic
inferred from title
author name string
Vincent J Starai
series ordinal
1
0 references
Christopher M Hickey
series ordinal
2
0 references
William Wickner
series ordinal
3
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language of work or name
English
0 references
publication date
June 2008
0 references
published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
18385512
retrieved
1 December 2016
volume
19
0 references
page(s)
2500-8
0 references
issue
6
0 references
cites work
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Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.
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Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
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Sec1p directly stimulates SNARE-mediated membrane fusion in vitro
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New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
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Sec1p binds to SNARE complexes and concentrates at sites of secretion
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A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
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Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
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Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
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A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
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SNAREpins: minimal machinery for membrane fusion
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SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
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The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation
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20 March 2017
Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
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Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
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20 March 2017
Membrane fusion
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7 April 2017
Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion
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Excess vacuolar SNAREs drive lysis and Rab bypass fusion
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29 September 2017
Assays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixing
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29 September 2017
Trans-SNARE complex assembly and yeast vacuole membrane fusion.
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29 September 2017
Reversible, cooperative reactions of yeast vacuole docking
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29 September 2017
SNARE-mediated lipid mixing depends on the physical state of the vesicles
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29 September 2017
Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion
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29 September 2017
Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
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29 September 2017
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
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29 September 2017
Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
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29 September 2017
Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae
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29 September 2017
Mosaic organization of the endocytic pathway
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29 September 2017
The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion
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29 September 2017
Exocytosis requires asymmetry in the central layer of the SNARE complex
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29 September 2017
Testing the 3Q:1R "rule": mutational analysis of the ionic "zero" layer in the yeast exocytic SNARE complex reveals no requirement for arginine
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29 September 2017
The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein
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Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs.
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G-protein ligands inhibit in vitro reactions of vacuole inheritance
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29 September 2017
Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
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2 June 2018
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Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p.
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A gain-of-function mutant of Munc18-1 stimulates secretory granule recruitment and exocytosis and reveals a direct interaction of Munc18-1 with Rab3
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12 December 2020
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Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. Isolation and characterization of two classes of vam mutants
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Membrane Trafficking: Three Steps to Fusion
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Identifiers
DOI
10.1091/MBC.E08-01-0077
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774560
OpenCitations bibliographic resource ID
1774560
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774560
PMCID
2397298
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774560
PubMed ID
18385512
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774560
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