HOPS recognizes each SNARE, assembling ternary trans -complexes for rapid fusion upon engagement with the 4th SNARE

Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs. HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a functional complex. Co-incubation of HOPS, proteo...

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Published ineLife Vol. 9
Main Authors Song, Hongki, Orr, Amy S, Lee, Miriam, Harner, Max E, Wickner, William T
Format Journal Article
LanguageEnglish
Published England eLife Science Publications, Ltd 21.01.2020
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Abstract Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs. HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a functional complex. Co-incubation of HOPS, proteoliposomes bearing R-SNARE, and proteoliposomes with any two Q-SNAREs yields a rapid-fusion complex with 3 SNAREs in a -assembly. The missing Q-SNARE then induces sudden fusion. HOPS can 'template' SNARE complex assembly through SM recognition of R- and Qa-SNAREs. Though the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS also assembles a rapid-fusion complex between R- and QbQc-SNARE proteoliposomes in the absence of Qa-SNARE, awaiting Qa for fusion. HOPS-dependent fusion is saturable at low concentrations of each Q-SNARE, showing binding site functionality. HOPS thus tethers membranes and recognizes each SNARE, assembling R+Qa or R+QbQc rapid fusion intermediates.
AbstractList Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs. HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a functional complex. Co-incubation of HOPS, proteoliposomes bearing R-SNARE, and proteoliposomes with any two Q-SNAREs yields a rapid-fusion complex with 3 SNAREs in a trans -assembly. The missing Q-SNARE then induces sudden fusion. HOPS can ‘template’ SNARE complex assembly through SM recognition of R- and Qa-SNAREs. Though the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS also assembles a rapid-fusion complex between R- and QbQc-SNARE proteoliposomes in the absence of Qa-SNARE, awaiting Qa for fusion. HOPS-dependent fusion is saturable at low concentrations of each Q-SNARE, showing binding site functionality. HOPS thus tethers membranes and recognizes each SNARE, assembling R+Qa or R+QbQc rapid fusion intermediates.
Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs. HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a functional complex. Co-incubation of HOPS, proteoliposomes bearing R-SNARE, and proteoliposomes with any two Q-SNAREs yields a rapid-fusion complex with 3 SNAREs in a trans-assembly. The missing Q-SNARE then induces sudden fusion. HOPS can ‘template’ SNARE complex assembly through SM recognition of R- and Qa-SNAREs. Though the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS also assembles a rapid-fusion complex between R- and QbQc-SNARE proteoliposomes in the absence of Qa-SNARE, awaiting Qa for fusion. HOPS-dependent fusion is saturable at low concentrations of each Q-SNARE, showing binding site functionality. HOPS thus tethers membranes and recognizes each SNARE, assembling R+Qa or R+QbQc rapid fusion intermediates.
Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs. HOPS catalyzes fusion when the Q-SNAREs are not pre-assembled, ushering them into a functional complex. Co-incubation of HOPS, proteoliposomes bearing R-SNARE, and proteoliposomes with any two Q-SNAREs yields a rapid-fusion complex with 3 SNAREs in a -assembly. The missing Q-SNARE then induces sudden fusion. HOPS can 'template' SNARE complex assembly through SM recognition of R- and Qa-SNAREs. Though the Qa-SNARE is essential for spontaneous SNARE assembly, HOPS also assembles a rapid-fusion complex between R- and QbQc-SNARE proteoliposomes in the absence of Qa-SNARE, awaiting Qa for fusion. HOPS-dependent fusion is saturable at low concentrations of each Q-SNARE, showing binding site functionality. HOPS thus tethers membranes and recognizes each SNARE, assembling R+Qa or R+QbQc rapid fusion intermediates.
Audience Academic
Author Orr, Amy S
Wickner, William T
Lee, Miriam
Song, Hongki
Harner, Max E
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Cites_doi 10.1038/sj.emboj.7601051
10.1038/nrm.2016.65
10.1038/nature14148
10.1006/prep.1998.1003
10.1083/jcb.136.2.307
10.1016/S0021-9258(19)37012-7
10.1091/mbc.E14-08-1298
10.1091/mbc.e13-07-0419
10.1038/sj.emboj.7600286
10.1083/jcb.108.5.1589
10.1038/sj.emboj.7600658
10.1038/35083000
10.1073/pnas.95.26.15781
10.1007/s00249-006-0097-z
10.1073/pnas.0908694106
10.1016/0092-8674(93)90376-2
10.1074/jbc.M111.307439
10.1038/35025084
10.1091/mbc.e11-02-0104
10.1146/annurev-cellbio-101011-155818
10.7554/eLife.03251
10.1016/S0092-8674(00)81404-X
10.7554/eLife.26646
10.1016/S0092-8674(02)00632-3
10.1038/26412
10.1091/mbc.e10-01-0044
10.1016/j.neuron.2013.10.022
10.1083/jcb.132.5.787
10.7554/eLife.38888
10.1091/mbc.e11-08-0680
10.7554/eLife.01879
10.1091/mbc.11.3.807
10.1091/mbc.e16-10-0743
10.1073/pnas.1907640116
10.1083/jcb.151.3.551
10.1083/jcb.200811082
10.1016/S0092-8674(00)81084-3
10.1074/jbc.272.17.11344
10.1074/jbc.M302003200
10.1126/science.aac7906
10.1091/mbc.e17-04-0218
10.1073/pnas.97.17.9402
10.1091/mbc.e16-07-0517
10.1073/pnas.0702290104
10.1074/jbc.m113.484410
10.1074/jbc.M109.045286
10.1073/pnas.1506409112
10.1083/jcb.200801001
10.1038/387199a0
10.1038/nature24469
10.1073/pnas.1216201109
10.1091/mbc.e16-04-0230
10.1021/ac60119a033
10.1083/jcb.200409068
10.7554/eLife.41771
10.1038/emboj.2008.139
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Keywords yeast vacuoles
chemical biology
biochemistry
HOPS
S. cerevisiae
SNARE
membrane fusion
Language English
License 2020, Song et al.
This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
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School of Life Sciences and Cell Logistics Research Center, Gwangju Institute of Science and Technology, Gwangju, Republic of Korea.
Biomedical Center Munich, Institute of Cardiovascular Physiology and Pathophysiology, Ludwig-Maximillians University Munich, Planegg-Martinsried, Germany.
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References Nakamura (bib24) 1997; 272
Wang (bib41) 2002; 108
Hickey (bib12) 2010; 21
Südhof (bib37) 2013; 80
Nichols (bib25) 1997; 387
Sutton (bib38) 1998; 395
Rizo (bib28) 2012; 28
Mayer (bib20) 2000; 11
Wickner (bib45) 2017; 28
Collins (bib6) 2005; 24
Zick (bib51) 2014; 3
Xu (bib48) 1996; 132
Weidman (bib43) 1989; 108
Lentz (bib17) 2007; 36
Krämer (bib16) 2011; 22
Song (bib34) 2017; 28
Mayer (bib21) 1997; 136
Zick (bib54) 2014; 3
Zick (bib52) 2015; 112
Brett (bib3) 2008; 182
Song (bib35) 2019; 116
Seals (bib30) 2000; 97
Izawa (bib13) 2012; 287
Cheever (bib4) 2001; 3
Söllner (bib32) 1993; 75
Zick (bib55) 2016; 27
Baker (bib2) 2016; 17
Fasshauer (bib9) 1998; 95
Zucchi (bib56) 2011; 22
Orr (bib27) 2017; 28
Song (bib33) 2017; 6
White (bib44) 2018; 7
Xu (bib49) 2012; 109
Wada (bib40) 1992; 267
Sheffield (bib31) 1999; 15
Zick (bib53) 2013; 24
Karunakaran (bib15) 2013; 268
D'Agostino (bib8) 2017; 551
Mima (bib22) 2008; 27
Zhao (bib50) 2015; 518
Fukuda (bib11) 2000; 407
Thorngren (bib39) 2004; 23
Schwartz (bib29) 2009; 185
Weber (bib42) 1998; 92
Mima (bib23) 2009; 106
Fratti (bib10) 2004; 167
Winter (bib46) 2009; 284
Stroupe (bib36) 2006; 25
Collins (bib7) 2007; 104
Wurmser (bib47) 2000; 151
Chen (bib5) 1956; 28
Jiao (bib14) 2018; 7
Marz (bib18) 2003; 278
Mayer (bib19) 1996; 85
Baker (bib1) 2015; 349
Orr (bib26) 2015; 26
References_xml – volume: 25
  start-page: 1579
  year: 2006
  ident: bib36
  article-title: Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
  publication-title: The EMBO Journal
  doi: 10.1038/sj.emboj.7601051
  contributor:
    fullname: Stroupe
– volume: 17
  start-page: 465
  year: 2016
  ident: bib2
  article-title: Chaperoning SNARE assembly and disassembly
  publication-title: Nature Reviews Molecular Cell Biology
  doi: 10.1038/nrm.2016.65
  contributor:
    fullname: Baker
– volume: 518
  start-page: 61
  year: 2015
  ident: bib50
  article-title: Mechanistic insights into the recycling machine of the SNARE complex
  publication-title: Nature
  doi: 10.1038/nature14148
  contributor:
    fullname: Zhao
– volume: 15
  start-page: 34
  year: 1999
  ident: bib31
  article-title: Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
  publication-title: Protein Expression and Purification
  doi: 10.1006/prep.1998.1003
  contributor:
    fullname: Sheffield
– volume: 136
  start-page: 307
  year: 1997
  ident: bib21
  article-title: Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.136.2.307
  contributor:
    fullname: Mayer
– volume: 267
  start-page: 18665
  year: 1992
  ident: bib40
  article-title: Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. isolation and characterization of two classes of vam mutants
  publication-title: The Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(19)37012-7
  contributor:
    fullname: Wada
– volume: 26
  start-page: 305
  year: 2015
  ident: bib26
  article-title: Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and rab:gtp for membrane binding and to catalyze tethering and fusion
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.E14-08-1298
  contributor:
    fullname: Orr
– volume: 24
  start-page: 3746
  year: 2013
  ident: bib53
  article-title: The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans -SNARE complexes
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e13-07-0419
  contributor:
    fullname: Zick
– volume: 23
  start-page: 2765
  year: 2004
  ident: bib39
  article-title: A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
  publication-title: The EMBO Journal
  doi: 10.1038/sj.emboj.7600286
  contributor:
    fullname: Thorngren
– volume: 108
  start-page: 1589
  year: 1989
  ident: bib43
  article-title: Binding of an N-ethylmaleimide-sensitive fusion protein to golgi membranes requires both a soluble protein(s) and an integral membrane receptor
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.108.5.1589
  contributor:
    fullname: Weidman
– volume: 24
  start-page: 1775
  year: 2005
  ident: bib6
  article-title: Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion
  publication-title: The EMBO Journal
  doi: 10.1038/sj.emboj.7600658
  contributor:
    fullname: Collins
– volume: 3
  start-page: 613
  year: 2001
  ident: bib4
  article-title: Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
  publication-title: Nature Cell Biology
  doi: 10.1038/35083000
  contributor:
    fullname: Cheever
– volume: 95
  start-page: 15781
  year: 1998
  ident: bib9
  article-title: Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
  publication-title: PNAS
  doi: 10.1073/pnas.95.26.15781
  contributor:
    fullname: Fasshauer
– volume: 36
  start-page: 315
  year: 2007
  ident: bib17
  article-title: PEG as a tool to gain insight into membrane fusion
  publication-title: European Biophysics Journal
  doi: 10.1007/s00249-006-0097-z
  contributor:
    fullname: Lentz
– volume: 106
  start-page: 16191
  year: 2009
  ident: bib23
  article-title: Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion
  publication-title: PNAS
  doi: 10.1073/pnas.0908694106
  contributor:
    fullname: Mima
– volume: 75
  start-page: 409
  year: 1993
  ident: bib32
  article-title: A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
  publication-title: Cell
  doi: 10.1016/0092-8674(93)90376-2
  contributor:
    fullname: Söllner
– volume: 287
  start-page: 3445
  year: 2012
  ident: bib13
  article-title: Distinct contributions of vacuolar qabc- and R-SNARE proteins to membrane fusion specificity
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M111.307439
  contributor:
    fullname: Izawa
– volume: 407
  start-page: 198
  year: 2000
  ident: bib11
  article-title: Functional architecture of an intracellular membrane t-SNARE
  publication-title: Nature
  doi: 10.1038/35025084
  contributor:
    fullname: Fukuda
– volume: 22
  start-page: 2601
  year: 2011
  ident: bib16
  article-title: HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e11-02-0104
  contributor:
    fullname: Krämer
– volume: 28
  start-page: 279
  year: 2012
  ident: bib28
  article-title: The membrane fusion enigma: snares, Sec1/Munc18 proteins, and their accomplices--guilty as charged?
  publication-title: Annual Review of Cell and Developmental Biology
  doi: 10.1146/annurev-cellbio-101011-155818
  contributor:
    fullname: Rizo
– volume: 3
  year: 2014
  ident: bib54
  article-title: A distinct tethering step is vital for vacuole membrane fusion
  publication-title: eLife
  doi: 10.7554/eLife.03251
  contributor:
    fullname: Zick
– volume: 92
  start-page: 759
  year: 1998
  ident: bib42
  article-title: SNAREpins: minimal machinery for membrane fusion
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81404-X
  contributor:
    fullname: Weber
– volume: 6
  year: 2017
  ident: bib33
  article-title: Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes
  publication-title: eLife
  doi: 10.7554/eLife.26646
  contributor:
    fullname: Song
– volume: 108
  start-page: 357
  year: 2002
  ident: bib41
  article-title: Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
  publication-title: Cell
  doi: 10.1016/S0092-8674(02)00632-3
  contributor:
    fullname: Wang
– volume: 395
  start-page: 347
  year: 1998
  ident: bib38
  article-title: Crystal structure of a SNARE complex involved in Synaptic exocytosis at 2.4 A resolution
  publication-title: Nature
  doi: 10.1038/26412
  contributor:
    fullname: Sutton
– volume: 21
  start-page: 2297
  year: 2010
  ident: bib12
  article-title: HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e10-01-0044
  contributor:
    fullname: Hickey
– volume: 80
  start-page: 675
  year: 2013
  ident: bib37
  article-title: Neurotransmitter release: the last millisecond in the life of a synaptic vesicle
  publication-title: Neuron
  doi: 10.1016/j.neuron.2013.10.022
  contributor:
    fullname: Südhof
– volume: 132
  start-page: 787
  year: 1996
  ident: bib48
  article-title: Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.132.5.787
  contributor:
    fullname: Xu
– volume: 7
  year: 2018
  ident: bib44
  article-title: Structural principles of SNARE complex recognition by the AAA+ protein NSF
  publication-title: eLife
  doi: 10.7554/eLife.38888
  contributor:
    fullname: White
– volume: 22
  start-page: 4635
  year: 2011
  ident: bib56
  article-title: Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e11-08-0680
  contributor:
    fullname: Zucchi
– volume: 3
  year: 2014
  ident: bib51
  article-title: Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion
  publication-title: eLife
  doi: 10.7554/eLife.01879
  contributor:
    fullname: Zick
– volume: 11
  start-page: 807
  year: 2000
  ident: bib20
  article-title: Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.11.3.807
  contributor:
    fullname: Mayer
– volume: 28
  start-page: 975
  year: 2017
  ident: bib27
  article-title: HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e16-10-0743
  contributor:
    fullname: Orr
– volume: 116
  start-page: 13952
  year: 2019
  ident: bib35
  article-title: Tethering guides fusion-competent trans-SNARE assembly
  publication-title: PNAS
  doi: 10.1073/pnas.1907640116
  contributor:
    fullname: Song
– volume: 151
  start-page: 551
  year: 2000
  ident: bib47
  article-title: New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.151.3.551
  contributor:
    fullname: Wurmser
– volume: 185
  start-page: 535
  year: 2009
  ident: bib29
  article-title: Capture and release of partially zipped trans-SNARE complexes on intact organelles
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.200811082
  contributor:
    fullname: Schwartz
– volume: 85
  start-page: 83
  year: 1996
  ident: bib19
  article-title: Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81084-3
  contributor:
    fullname: Mayer
– volume: 272
  start-page: 11344
  year: 1997
  ident: bib24
  article-title: Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.272.17.11344
  contributor:
    fullname: Nakamura
– volume: 278
  start-page: 27000
  year: 2003
  ident: bib18
  article-title: Defining the SNARE complex binding surface of alpha-SNAP: implications for SNARE complex disassembly
  publication-title: The Journal of Biological Chemistry
  doi: 10.1074/jbc.M302003200
  contributor:
    fullname: Marz
– volume: 349
  start-page: 1111
  year: 2015
  ident: bib1
  article-title: A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
  publication-title: Science
  doi: 10.1126/science.aac7906
  contributor:
    fullname: Baker
– volume: 28
  start-page: 2282
  year: 2017
  ident: bib34
  article-title: A short region upstream of the yeast vacuolar Qa-SNARE heptad-repeats promotes membrane fusion through enhanced SNARE complex assembly
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e17-04-0218
  contributor:
    fullname: Song
– volume: 97
  start-page: 9402
  year: 2000
  ident: bib30
  article-title: A ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
  publication-title: PNAS
  doi: 10.1073/pnas.97.17.9402
  contributor:
    fullname: Seals
– volume: 28
  start-page: 707
  year: 2017
  ident: bib45
  article-title: A cascade of multiple proteins and lipids catalyzes membrane fusion
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e16-07-0517
  contributor:
    fullname: Wickner
– volume: 104
  start-page: 8755
  year: 2007
  ident: bib7
  article-title: Trans-SNARE complex assembly and yeast vacuole membrane fusion
  publication-title: PNAS
  doi: 10.1073/pnas.0702290104
  contributor:
    fullname: Collins
– volume: 268
  start-page: 28557
  year: 2013
  ident: bib15
  article-title: Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p
  publication-title: The Journal of Biological Chemistry
  doi: 10.1074/jbc.m113.484410
  contributor:
    fullname: Karunakaran
– volume: 284
  start-page: 31817
  year: 2009
  ident: bib46
  article-title: A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M109.045286
  contributor:
    fullname: Winter
– volume: 112
  start-page: E2290
  year: 2015
  ident: bib52
  article-title: Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18
  publication-title: PNAS
  doi: 10.1073/pnas.1506409112
  contributor:
    fullname: Zick
– volume: 182
  start-page: 1141
  year: 2008
  ident: bib3
  article-title: Efficient termination of vacuolar rab GTPase signaling requires coordinated action by a GAP and a protein kinase
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.200801001
  contributor:
    fullname: Brett
– volume: 387
  start-page: 199
  year: 1997
  ident: bib25
  article-title: Homotypic vacuolar fusion mediated by t- and v-SNAREs
  publication-title: Nature
  doi: 10.1038/387199a0
  contributor:
    fullname: Nichols
– volume: 551
  start-page: 634
  year: 2017
  ident: bib8
  article-title: A tethering complex drives the terminal stage of SNARE-dependent membrane fusion
  publication-title: Nature
  doi: 10.1038/nature24469
  contributor:
    fullname: D'Agostino
– volume: 109
  start-page: 17936
  year: 2012
  ident: bib49
  article-title: N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly
  publication-title: PNAS
  doi: 10.1073/pnas.1216201109
  contributor:
    fullname: Xu
– volume: 27
  start-page: 2590
  year: 2016
  ident: bib55
  article-title: Improved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement
  publication-title: Molecular Biology of the Cell
  doi: 10.1091/mbc.e16-04-0230
  contributor:
    fullname: Zick
– volume: 28
  start-page: 1756
  year: 1956
  ident: bib5
  article-title: Microdetermination of phosphorus
  publication-title: Analytical Chemistry
  doi: 10.1021/ac60119a033
  contributor:
    fullname: Chen
– volume: 167
  start-page: 1087
  year: 2004
  ident: bib10
  article-title: Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
  publication-title: The Journal of Cell Biology
  doi: 10.1083/jcb.200409068
  contributor:
    fullname: Fratti
– volume: 7
  year: 2018
  ident: bib14
  article-title: Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association
  publication-title: eLife
  doi: 10.7554/eLife.41771
  contributor:
    fullname: Jiao
– volume: 27
  start-page: 2031
  year: 2008
  ident: bib22
  article-title: Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
  publication-title: The EMBO Journal
  doi: 10.1038/emboj.2008.139
  contributor:
    fullname: Mima
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Snippet Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four...
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SourceType Open Website
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Aggregation Database
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SubjectTerms Binding sites
Biochemistry and Chemical Biology
HOPS
Intermediates
Intracellular Membranes - metabolism
Lipids
Membrane Fusion
Membranes
Protein Binding
Proteins
Questions and answers
R-SNARE Proteins - metabolism
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
SNAP receptors
SNARE
Vacuoles - metabolism
yeast vacuoles
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Title HOPS recognizes each SNARE, assembling ternary trans -complexes for rapid fusion upon engagement with the 4th SNARE
URI https://www.ncbi.nlm.nih.gov/pubmed/31961324
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https://pubmed.ncbi.nlm.nih.gov/PMC6994237
https://doaj.org/article/96ca243ac1224bc9b3276c51a02beeec
Volume 9
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