Distinct features of multivesicular body-lysosome fusion revealed by a new cell-free content-mixing assay

When marked for degradation, surface receptor and transporter proteins are internalized and delivered to endosomes where they are packaged into intralumenal vesicles (ILVs). Many rounds of ILV formation create multivesicular bodies (MVBs) that fuse with lysosomes exposing ILVs to hydrolases for cata...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:bioRxiv
Hlavní autoři: Mahmoud Abdul Karim, Samyn, Dieter Ronny, Mattie, Sevan, Christopher Leonard Brett
Médium: Paper
Jazyk:angličtina
Vydáno: Cold Spring Harbor Cold Spring Harbor Laboratory Press 27.10.2017
Cold Spring Harbor Laboratory
Vydání:1.2
Témata:
ISSN:2692-8205, 2692-8205
On-line přístup:Získat plný text
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Abstract When marked for degradation, surface receptor and transporter proteins are internalized and delivered to endosomes where they are packaged into intralumenal vesicles (ILVs). Many rounds of ILV formation create multivesicular bodies (MVBs) that fuse with lysosomes exposing ILVs to hydrolases for catabolism. Despite being critical for protein degradation, the molecular underpinnings of MVB-lysosome fusion remain unclear, although machinery underlying other lysosome fusion events is implicated. But how then is specificity conferred? And how is MVB maturation and fusion coordinated for efficient protein degradation? To address these questions, we developed a cell-free MVB-lysosome fusion assay using S. cerevisiae as a model. After confirming that the Rab7 ortholog Ypt7 and the multisubunit tethering complex HOPS are required, we found that the Qa-SNARE Pep12 distinguishes this event from homotypic lysosome fusion. Mutations that impair MVB maturation block fusion by preventing Ypt7 activation, confirming that a Rab-cascade mechanism harmonizes MVB maturation with lysosome fusion.
AbstractList When marked for degradation, surface receptor and transporter proteins are internalized and delivered to endosomes where they are packaged into intralumenal vesicles (ILVs). Many rounds of ILV formation create multivesicular bodies (MVBs) that fuse with lysosomes exposing ILVs to hydrolases for catabolism. Despite being critical for protein degradation, the molecular underpinnings of MVB-lysosome fusion remain unclear, although machinery underlying other lysosome fusion events is implicated. But how then is specificity conferred? And how is MVB maturation and fusion coordinated for efficient protein degradation? To address these questions, we developed a cell-free MVB-lysosome fusion assay using S. cerevisiae as a model. After confirming that the Rab7 ortholog Ypt7 and the multisubunit tethering complex HOPS are required, we found that the Qa-SNARE Pep12 distinguishes this event from homotypic lysosome fusion. Mutations that impair MVB maturation block fusion by preventing Ypt7 activation, confirming that a Rab-cascade mechanism harmonizes MVB maturation with lysosome fusion. Endocytosis culminates with multivesicular bodies (MVBs) fusing with lysosomes. But the molecular underpinnings of this event remain unclear. Here, using S. cerevisiae as a model, Karim et al. employ a new in vitro assay to show that MVB-lysosome fusion is driven by ESCRT-dependent Rab-GTPase activation and the syntaxin ortholog Pep12, distinguishing it from other lysosome membrane fusion events.
When marked for degradation, surface receptor and transporter proteins are internalized and delivered to endosomes where they are packaged into intralumenal vesicles (ILVs). Many rounds of ILV formation create multivesicular bodies (MVBs) that fuse with lysosomes exposing ILVs to hydrolases for catabolism. Despite being critical for protein degradation, the molecular underpinnings of MVB-lysosome fusion remain unclear, although machinery underlying other lysosome fusion events is implicated. But how then is specificity conferred? And how is MVB maturation and fusion coordinated for efficient protein degradation? To address these questions, we developed a cell-free MVB-lysosome fusion assay using S. cerevisiae as a model. After confirming that the Rab7 ortholog Ypt7 and the multisubunit tethering complex HOPS are required, we found that the Qa-SNARE Pep12 distinguishes this event from homotypic lysosome fusion. Mutations that impair MVB maturation block fusion by preventing Ypt7 activation, confirming that a Rab-cascade mechanism harmonizes MVB maturation with lysosome fusion.
Author Mahmoud Abdul Karim
Mattie, Sevan
Samyn, Dieter Ronny
Christopher Leonard Brett
Author_xml – sequence: 1
  fullname: Mahmoud Abdul Karim
– sequence: 2
  givenname: Dieter
  surname: Samyn
  middlename: Ronny
  fullname: Samyn, Dieter Ronny
– sequence: 3
  givenname: Sevan
  surname: Mattie
  fullname: Mattie, Sevan
– sequence: 4
  fullname: Christopher Leonard Brett
BookMark eNpNkF1LwzAYhYNMcM75D4SA19V8tE16KfMTBt7sviTpG8lok5mkdf33DuaFV-fAAw-Hc40WPnhA6JaSB0oJfaScE1FeoCWrG1ZIRqrFv36F1intCSGsqSkX5RK5Z5ey8yZjCyqPERIOFg9jn90EyZmxVxHr0M1FP6eQwgDYjskFjyNMoHrosJ6xwh5-sIG-L2wEwCb4DD4Xgzs6_4VVSmq-QZdW9QnWf7lCu9eX3ea92H6-fWyetoWWrCyEoVoCJ6VSnRUd6NoQKzlQYUqpiDWyahpghtWkk0Rq1WhLtbCVoI1l2vAVujtrtQvx6Kb2EN2g4tyenznx-zM_xPA9QsrtPozRnxa1jAjKKs6I5L85rGW4
Cites_doi 10.1016/0092-8674(94)90219-4
10.1091/mbc.E12-05-0343
10.1016/j.ceb.2009.05.007
10.1073/pnas.97.17.9402
10.1016/S0092-8674(01)00434-2
10.1101/167411
10.1242/jcs.071977
10.1128/MCB.8.11.4936.Updated
10.1083/jcb.200409068
10.1111 /tra.12283
10.1093/emboj/19.24.6713
10.1083/jcb.200801001
10.1038/387199a0
10.1146/annurev-cellbio-100109-104131
10.1016/j.devcel.2011.05.015
10.1515/hsz-2013-0258
10.1083/jcb.137.7.1511
10.1016/j.ceb.2014.04.007
10.1242/jcs.107805
10.1016/j.devcel.2007.03.006
10.1091/mbc.E09
10.1091/mbc.E04-05-0420
10.1083/jcb.140.1.61
10.1016/S0092-8674(00)81084-3
10.1038/sj.emboj.7600286
10.1016/j.cub.2012.01.028
10.1111/j.1600-0854.2009.00920.x
10.1126/science.aac7906
10.1101/170175
10.1091/mbc.E14-06-1156
10.1242/jcs.111310
10.1038/emboj.2011.286
10.1083/jcb.200811082
10.1007/BF00986234
10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
10.1083/jcb.119.6.1469
10.1111/tra.12027
10.1091/mbc.E15-02-0062
10.1016/S0014-5793(97)00575-9
10.1042/BST0381413
10.1042/BST0381469
10.1091/mbc.3.12.1389
10.1146/annurev.cellbio.23.090506.123319
10.1042/BST0370167
tra020705 [pii]
10.1038/srep04277
10.1091/mbc.E08
10.1091/mbc.E03-10-0767
10.1073/pnas.0700970104
10.1073/pnas.0702290104
10.1016/j.cub.2008.06.050
ContentType Paper
Copyright 2017. Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the associated terms available at https://www.biorxiv.org/content/early/2017/10/27/133074
2017, Posted by Cold Spring Harbor Laboratory
Copyright_xml – notice: 2017. Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the associated terms available at https://www.biorxiv.org/content/early/2017/10/27/133074
– notice: 2017, Posted by Cold Spring Harbor Laboratory
DBID 8FE
8FH
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
GNUQQ
HCIFZ
LK8
M7P
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
FX.
DOI 10.1101/133074
DatabaseName ProQuest SciTech Collection
ProQuest Natural Science Collection
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
Biological Science Database
AUTh Library subscriptions: ProQuest Central
Natural Science Collection
ProQuest One Community College
ProQuest Central Korea
ProQuest Central Student
SciTech Premium Collection
ProQuest Biological Science Collection
ProQuest Biological Science
ProQuest Central Premium
ProQuest One Academic
ProQuest Publicly Available Content
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic (retired)
ProQuest One Academic UKI Edition
ProQuest Central China
bioRxiv
DatabaseTitle Publicly Available Content Database
ProQuest Central Student
ProQuest One Academic Middle East (New)
ProQuest Biological Science Collection
ProQuest Central Essentials
ProQuest One Academic Eastern Edition
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
Biological Science Database
ProQuest SciTech Collection
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
ProQuest One Academic UKI Edition
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Central (New)
ProQuest One Academic
ProQuest One Academic (New)
DatabaseTitleList
Publicly Available Content Database
Database_xml – sequence: 1
  dbid: PIMPY
  name: Publicly Available Content Database
  url: http://search.proquest.com/publiccontent
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2692-8205
Edition 1.2
ExternalDocumentID 133074v2
Genre Working Paper/Pre-Print
GroupedDBID 8FE
8FH
ABUWG
AFKRA
ALMA_UNASSIGNED_HOLDINGS
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
GNUQQ
HCIFZ
LK8
M7P
NQS
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
PROAC
RHI
FX.
ID FETCH-LOGICAL-b824-7c1b8e304aadf7deb6c0f83e17c48a0fc8599e2c260d808ba9bf1b7f5719f2bc3
IEDL.DBID M7P
ISSN 2692-8205
IngestDate Tue Jan 07 18:51:37 EST 2025
Fri Jul 25 09:13:59 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed false
IsScholarly false
Keywords Rab7
vacuole
ESCRT
Rab-GTPase
Pep12
SNARE
membrane fusion
Ypt7
Rab conversion
syntaxin
multivesicular body
MVB
endocytosis
lysosome
Language English
License The copyright holder for this pre-print is the author. All rights reserved. The material may not be redistributed, re-used or adapted without the author's permission.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-b824-7c1b8e304aadf7deb6c0f83e17c48a0fc8599e2c260d808ba9bf1b7f5719f2bc3
Notes SourceType-Working Papers-1
ObjectType-Working Paper/Pre-Print-1
content type line 50
OpenAccessLink https://www.proquest.com/docview/2071253208?pq-origsite=%requestingapplication%
PQID 2071253208
PQPubID 2050091
PageCount 32
ParticipantIDs biorxiv_primary_133074
proquest_journals_2071253208
PublicationCentury 2000
PublicationDate 20171027
PublicationDateYYYYMMDD 2017-10-27
PublicationDate_xml – month: 10
  year: 2017
  text: 20171027
  day: 27
PublicationDecade 2010
PublicationPlace Cold Spring Harbor
PublicationPlace_xml – name: Cold Spring Harbor
PublicationTitle bioRxiv
PublicationYear 2017
Publisher Cold Spring Harbor Laboratory Press
Cold Spring Harbor Laboratory
Publisher_xml – name: Cold Spring Harbor Laboratory Press
– name: Cold Spring Harbor Laboratory
References Wickner (133074v2.74) 2010; 26
Peterson, Emr (133074v2.48) 2001; 2
Becherer, Rieder, Emr, Jones (133074v2.4) 1996; 7
Nordmann, Cabrera, Perz, Bröcker, Ostrowicz, Engelbrecht-Vandré, Ungermann (133074v2.45) 2010; 20
Gossing, Chidambaram, Fischer von Mollard (133074v2.23) 2013; 8
Ungermann, Fischer von Mollard, Jensen, Margolis, Stevens, Wickner (133074v2.68) 1999; 145
Balderhaar, Ungermann (133074v2.3) 2013; 126
Marcusson, Horazdovsky, Cereghino, Gharakhanian, Emr (133074v2.37) 1994; 77
Peplowska, Markgraf, Ostrowicz, Bange, Ungermann (133074v2.47) 2007; 12
Cowles, Odorizzi, Payne, Emr (133074v2.13) 1997; 91
Futter, Pearse, Hewlett, Hopkins (133074v2.21) 1996; 132
Piper, Katzmann (133074v2.49) 2007; 23
Wartosch, Gunesdogan, Graham, Luzio (133074v2.72) 2015
Bugnicourt, Froissard, Sereti, Ulrich, Haguenauer-Tsapis, Galan (133074v2.7) 2004; 15
Schmidt, Teis (133074v2.59) 2012; 22
Huotari, Helenius (133074v2.28) 2011; 30
Thorngren, Collins, Fratti, Wickner, Merz (133074v2.66) 2004; 23
Dietrich, Peplowska, LaGrassa, Hou, Rohde, Ungermann (133074v2.15) 2005; 6
Furukawa, Mima (133074v2.20) 2014; 4
Pols, Ten Brink, Gosavi, Oorschot, Klumperman (133074v2.51) 2013; 14
Balderhaar, Arlt, Ostrowicz, Bröcker, Sündermann, Brandt, Babst, Ungermann (133074v2.2) 2010; 123
Mattie, McNally, Karim, Vali, Brett (133074v2.38) 2017; 28
McNally, Brett (133074v2.40) 2017; 25
Wickner, Rizo (133074v2.75) 2017; 28
Subramanian (133074v2.65) 2004; 15
Rana, Lachmann, Ungermann (133074v2.53) 2015; 26
Cao, Zhong, Zou, Murrell-Lagnado, Zhu, Dong (133074v2.9) 2015; 209
Lobingier, Merz (133074v2.34) 2012; 23
Dennis, Delevoye, Acosta-Ruiz, Hurbain, Romao, Hesketh, Goff, Sviderskaya, Bennett, Luzio, Galli, Owen, Raposo, Marks (133074v2.14) 2016; 214
Starai, Hlckey, Wickner (133074v2.63) 2008; 19
Pryor, Mullock, Bright, Lindsay, Gray, Richardson, Stewart, James, Piper, Luzio (133074v2.52) 2004; 5
Brett, Plemel, Lobinger, Vignali, Fields, Merz (133074v2.6) 2008; 182
Rivera-Molina, Novick (133074v2.55) 2009; 106
Kümmel, Ungermann (133074v2.32) 2014; 29
Metcalf, Isaacs (133074v2.41) 2010; 38
Morvan, Köchl, Watson, Collinson, Jefferies, Tooze (133074v2.42) 2009; 5
Wang, Seeley, Wickner, Merz (133074v2.70) 2002; 108
Lachmann, Barr, Ungermann (133074v2.33) 2012; 23
Wen, Chen, Wu, Sun, Zhang, Banfield (133074v2.73) 2006; 17
Ungermann, Nichols, Pelham, Wickner (133074v2.67) 1998; 140
Saksena, Emr (133074v2.58) 2009; 37
Robinson, Klionsky, Banta, Emr (133074v2.56) 1988; 8
Eitzen, Will, Gallwitz, Haas, Wickner (133074v2.16) 2000; 19
Stuffers, Sem Wegner, Stenmark, Brech (133074v2.64) 2009; 10
Vida, Gerhardt (133074v2.69) 1999; 146
Russell, Shideler, Nickerson, West, Odorizzi (133074v2.57) 2012; 125
Wang, Merz, Collins, Wickner (133074v2.71) 2003; 160
Luzio, Gray, Bright (133074v2.36) 2010; 38
Shideler, Nickerson, Merz, Odorizzi (133074v2.62) 2015; 26
Longtine, McKenzie, Demarini, Shah, Wach, Brachat, Philippsen, Pringle (133074v2.35) 1998; 14
Schwartz, Merz (133074v2.60) 2009; 185
Cabrera, Ostrowicz, Mari, LaGrassa, Reggiori, Ungermann (133074v2.8) 2009; 20
Götte, Gallwitz (133074v2.24) 1997; 411
Plemel, Lobingier, Brett, Angers, Nickerson, Paulsel, Sprague, Merz (133074v2.50) 2011; 22
Seals, Eitzen, Margolis, Wickner, Price (133074v2.61) 2000; 97
Collins, Wickner (133074v2.10) 2007; 104
Coonrod, Stevens (133074v2.12) 2010; 21
Nickerson, Brett, Merz (133074v2.44) 2009; 21
Numrich, Ungermann (133074v2.46) 2014; 395
Baker, Jeffrey, Zick, Phillips, Wickner, Hughson (133074v2.1) 2015; 349
Brett, Merz (133074v2.5) 2008; 18
Mayer, Wickner, Haas (133074v2.39) 1996; 85
Karim, Brett (133074v2.30) 2017
Nichols, Ungermann, Pelham, Wickner, Haas (133074v2.43) 1997; 387
Conradt, Shaw, Vida, Emr, Wickner (133074v2.11) 1992; 119
Fischer von Mollard, Nothwehr, Stevens (133074v2.18) 1997; 137
Jun, Wickner (133074v2.29) 2007; 104
Gurunathan, Chapman-Shimshoni, Trajkovic, Gerst (133074v2.25) 2000; 11
Henne, Buchkovich, Emr (133074v2.27) 2011; 21
Fischer von Mollard, Stevens (133074v2.17) 1999; 10
Fratti, Jun, Merz, Margolis, Wickner, Wickner (133074v2.19) 2004; 167
Gerrard, Levi, Stevens (133074v2.22) 2000; 1
Haas (133074v2.26) 1995; 17
Raymond, Howald-Stevenson, Vater, Stevens (133074v2.54) 1992; 3
Katzmann, Babst, Emr (133074v2.31) 2001; 106
References_xml – volume: 77
  start-page: 579
  year: 1994
  end-page: 586
  ident: 133074v2.37
  article-title: The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
  publication-title: Cell.
  doi: 10.1016/0092-8674(94)90219-4
– volume: 23
  start-page: 2516
  year: 2012
  end-page: 2526
  ident: 133074v2.33
  article-title: The Msb3/Gyp3 GAP controls the activity of the Rab GTPase Vps21 and Ypt7 at endosomes and vacuoles
  publication-title: Mol. Biol. Cell.
– volume: 17
  start-page: 4282
  year: 2006
  end-page: 4299
  ident: 133074v2.73
  article-title: Identification of the yeast R-SNARE Nyv1 as a novel longin domain-containing protein
  publication-title: Mol. Biol. Cell.
– volume: 23
  start-page: 4611
  year: 2012
  end-page: 22
  ident: 133074v2.34
  article-title: Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E12-05-0343
– volume: 21
  start-page: 543
  year: 2009
  end-page: 551
  ident: 133074v2.44
  article-title: Vps-C complexes: gatekeepers of endolysosomal traffic
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/j.ceb.2009.05.007
– volume: 97
  start-page: 9402
  year: 2000
  end-page: 9407
  ident: 133074v2.61
  article-title: A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.97.17.9402
– volume: 106
  start-page: 145
  year: 2001
  end-page: 155
  ident: 133074v2.31
  article-title: Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
  publication-title: Cell.
  doi: 10.1016/S0092-8674(01)00434-2
– volume: 25
  start-page: 167411
  year: 2017
  ident: 133074v2.40
  article-title: ESCRT-independent surface receptor and transporter protein degradation by the ILF pathway
  publication-title: bioRxiv
  doi: 10.1101/167411
– volume: 123
  start-page: 4085
  year: 2010
  end-page: 4094
  ident: 133074v2.2
  article-title: The Rab GTPase Ypt7 is linked to retromer-mediated receptor recycling and fusion at the yeast late endosome
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.071977
– volume: 8
  start-page: 4936
  year: 1988
  end-page: 4948
  ident: 133074v2.56
  article-title: Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.8.11.4936.Updated
– volume: 167
  start-page: 1087
  year: 2004
  end-page: 1098
  ident: 133074v2.19
  article-title: Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200409068
– start-page: 727
  year: 2015
  end-page: 742
  ident: 133074v2.72
  article-title: Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes
  publication-title: Traffic
  doi: 10.1111 /tra.12283
– volume: 19
  start-page: 6713
  year: 2000
  end-page: 6720
  ident: 133074v2.16
  article-title: Sequential action of two GTPases to promote vacuole docking and fusion
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.24.6713
– volume: 182
  start-page: 1141
  year: 2008
  end-page: 1151
  ident: 133074v2.6
  article-title: Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200801001
– volume: 387
  start-page: 199
  year: 1997
  end-page: 202
  ident: 133074v2.43
  article-title: Homotypic vacuolar fusion mediated by t- and v-SNAREs
  publication-title: Nature.
  doi: 10.1038/387199a0
– volume: 26
  start-page: 115
  year: 2010
  end-page: 136
  ident: 133074v2.74
  article-title: Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles
  publication-title: Annu. Rev. Cell Dev. Biol.
  doi: 10.1146/annurev-cellbio-100109-104131
– volume: 214
  start-page: 293
  year: 2016
  end-page: 308
  ident: 133074v2.14
  article-title: BLOC-1 and BLOC-3 regulate VAMP7 cycling to and from melanosomes via distinct tubular transport carriers
  publication-title: J. Cell Biol.
– volume: 21
  start-page: 77
  year: 2011
  end-page: 91
  ident: 133074v2.27
  article-title: The ESCRT Pathway
  publication-title: Dev. Cell.
  doi: 10.1016/j.devcel.2011.05.015
– volume: 28
  start-page: 707
  year: 2017
  end-page: 711
  ident: 133074v2.75
  article-title: A cascade of multiple proteins and lipids catalyzes membrane fusion
  publication-title: Mol. Biol. Cell.
– volume: 146
  start-page: 85
  year: 1999
  end-page: 98
  ident: 133074v2.69
  article-title: A cell-free assay allows reconstitution of Vps33p-dependent transport to the yeast vacuole/lysosome
  publication-title: J. Cell. Biol.
– volume: 395
  start-page: 327
  year: 2014
  end-page: 333
  ident: 133074v2.46
  article-title: Endocytic Rabs in membrane trafficking and signaling
  publication-title: Biol. Chem.
  doi: 10.1515/hsz-2013-0258
– volume: 137
  start-page: 1511
  year: 1997
  end-page: 1524
  ident: 133074v2.18
  article-title: The yeast V-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.137.7.1511
– volume: 29
  start-page: 61
  year: 2014
  end-page: 66
  ident: 133074v2.32
  article-title: Principles of membrane tethering and fusion in endosome and lysosome biogenesis
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/j.ceb.2014.04.007
– volume: 126
  start-page: 1307
  year: 2013
  end-page: 16
  ident: 133074v2.3
  article-title: CORVET and HOPS tethering complexes - coordinators of endosome and lysosome fusion
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.107805
– volume: 20
  start-page: 1654
  year: 2010
  end-page: 1659
  ident: 133074v2.45
  article-title: The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7
  publication-title: Curr. Biol.
– volume: 20
  start-page: 1937
  year: 2009
  end-page: 1948
  ident: 133074v2.8
  article-title: Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites
  publication-title: Mol. Biol. Cell.
– volume: 12
  start-page: 739
  year: 2007
  end-page: 750
  ident: 133074v2.47
  article-title: The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis
  publication-title: Dev. Cell.
  doi: 10.1016/j.devcel.2007.03.006
– volume: 106
  start-page: 14408
  year: 2009
  end-page: 14413
  ident: 133074v2.55
  article-title: A Rab GAP cascade defines the boundary between two RabGTPases on the secretory pathway
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
– volume: 21
  start-page: 4042
  year: 2010
  end-page: 4056
  ident: 133074v2.12
  article-title: The Yeast vps Class E Mutants: The Beginning of the Molecular Genetic Analysis of Multivesicular Body Biogenesis
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E09
– volume: 22
  start-page: 1353
  year: 2011
  end-page: 63
  ident: 133074v2.50
  article-title: Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic
  publication-title: Mol. Biol. Cell.
– volume: 11
  start-page: 3629
  year: 2000
  end-page: 3643
  ident: 133074v2.25
  article-title: Yeast exocytic v-SNAREs confer endocytosis
  publication-title: Mol. Biol. Cell.
– volume: 15
  start-page: 4203
  year: 2004
  end-page: 14
  ident: 133074v2.7
  article-title: Antagonistic roles of ESCRT and Vps class C/HOPS complexes in the recycling of yeast membrane proteins
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E04-05-0420
– volume: 91
  start-page: 109
  year: 1997
  end-page: 118
  ident: 133074v2.13
  article-title: The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
  publication-title: Cell.
– volume: 140
  start-page: 61
  year: 1998
  end-page: 69
  ident: 133074v2.67
  article-title: A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.140.1.61
– volume: 85
  start-page: 83
  year: 1996
  end-page: 94
  ident: 133074v2.39
  article-title: Sec18p (NSF)-driven release of Sec17p (a-SNAP) can precede docking and fusion of yeast vacuoles
  publication-title: Cell.
  doi: 10.1016/S0092-8674(00)81084-3
– volume: 209
  start-page: 879
  year: 2015
  end-page: 894
  ident: 133074v2.9
  article-title: Calcium release through P2X4 activates calmodulin to promote endolysosomal membrane fusion
  publication-title: J. Cell Biol.
– volume: 23
  start-page: 2765
  year: 2004
  end-page: 2776
  ident: 133074v2.66
  article-title: A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7600286
– volume: 22
  year: 2012
  ident: 133074v2.59
  article-title: The ESCRT machinery
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2012.01.028
– volume: 160
  start-page: 365
  year: 2003
  end-page: 374
  ident: 133074v2.71
  article-title: Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
  publication-title: J. Cell Biol.
– volume: 10
  start-page: 925
  year: 2009
  end-page: 937
  ident: 133074v2.64
  article-title: Multivesicular endosome biogenesis in the absence of ESCRTs
  publication-title: Traffic.
  doi: 10.1111/j.1600-0854.2009.00920.x
– volume: 349
  start-page: 1111
  year: 2015
  end-page: 1114
  ident: 133074v2.1
  article-title: A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
  publication-title: Science (80-.).
  doi: 10.1126/science.aac7906
– year: 2017
  ident: 133074v2.30
  article-title: The Na+(K+)/H+ exchanger Nhx1 controls multivesicular body-vacuolar lysosome fusion
  publication-title: bioRxiv
  doi: 10.1101/170175
– volume: 145
  start-page: 1435
  year: 1999
  end-page: 1442
  ident: 133074v2.68
  article-title: Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion
  publication-title: J. Cell Biol.
– volume: 26
  start-page: 1345
  year: 2015
  end-page: 56
  ident: 133074v2.62
  article-title: Ubiquitin binding by the CUE domain promotes endosomal localization of the Rab5 GEF Vps9
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E14-06-1156
– volume: 125
  start-page: 5208
  year: 2012
  end-page: 20
  ident: 133074v2.57
  article-title: Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.111310
– volume: 30
  start-page: 3481
  year: 2011
  end-page: 3500
  ident: 133074v2.28
  article-title: Endosome maturation
  publication-title: EMBO J.
  doi: 10.1038/emboj.2011.286
– volume: 1
  start-page: 259
  year: 2000
  end-page: 269
  ident: 133074v2.22
  article-title: Pep12p is a multifunctional yeast syntaxin that controls entry of biosynthetic, endocytic and retrograde traffic into the prevacuolar compartment
  publication-title: Traffic
– volume: 185
  start-page: 535
  year: 2009
  end-page: 49
  ident: 133074v2.60
  article-title: Capture and release of partially zipped trans-SNARE complexes on intact organelles
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200811082
– volume: 17
  start-page: 283
  year: 1995
  end-page: 294
  ident: 133074v2.26
  article-title: A quantitative assay to measure homotypic vacuole fusion in vitro
  publication-title: Methods Cell Sci.
  doi: 10.1007/BF00986234
– volume: 14
  start-page: 953
  year: 1998
  end-page: 961
  ident: 133074v2.35
  article-title: Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
  publication-title: Yeast.
  doi: 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
– volume: 119
  start-page: 1469
  year: 1992
  end-page: 1479
  ident: 133074v2.11
  article-title: In vitro reactions of vacuole inheritance in Saccharomyces cerevisiae
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.119.6.1469
– volume: 14
  start-page: 219
  year: 2013
  end-page: 232
  ident: 133074v2.51
  article-title: The HOPS Proteins hVps41 and hVps39 Are Required for Homotypic and Heterotypic Late Endosome Fusion
  publication-title: Traffic.
  doi: 10.1111/tra.12027
– volume: 8
  start-page: e66304
  year: 2013
  ident: 133074v2.23
  article-title: Importance of the N-terminal domain of the Qb-SNARE Vti1 p for different membrane transport steps in the yeast endosomal system
  publication-title: PLoS One.
– volume: 26
  start-page: 2535
  year: 2015
  end-page: 49
  ident: 133074v2.53
  article-title: Identification of a Rab GAP cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E15-02-0062
– volume: 411
  start-page: 48
  year: 1997
  end-page: 52
  ident: 133074v2.24
  article-title: High expression of the yeast syntaxin-related Vam3 protein suppresses the protein transport defects of a pep12 null mutant
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(97)00575-9
– volume: 5
  start-page: 590
  year: 2004
  end-page: 595
  ident: 133074v2.52
  article-title: Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late endocytic fusion events
  publication-title: EMBO Rep.
– volume: 6
  start-page: 245
  year: 2005
  end-page: 250
  ident: 133074v2.15
  article-title: The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion
  publication-title: EMBO Rep
– volume: 28
  start-page: 309
  year: 2017
  end-page: 321
  ident: 133074v2.38
  article-title: How and why intralumenal membrane fragments form during vacuolar lysosome fusion
  publication-title: Mol. Biol. Cell.
– volume: 132
  start-page: 1011
  year: 1996
  end-page: 1023
  ident: 133074v2.21
  article-title: Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature then fuse directly with lysosomes
  publication-title: J. Cell Biol
– volume: 38
  start-page: 14131416
  year: 2010
  ident: 133074v2.36
  article-title: Endosome-lysosome fusion
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0381413
– volume: 38
  start-page: 1469
  year: 2010
  end-page: 1473
  ident: 133074v2.41
  article-title: The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0381469
– volume: 3
  start-page: 1389
  year: 1992
  end-page: 402
  ident: 133074v2.54
  article-title: Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.3.12.1389
– volume: 23
  start-page: 519
  year: 2007
  end-page: 47
  ident: 133074v2.49
  article-title: Biogenesis and function of multivesicular bodies
  publication-title: Annu. Rev. Cell Dev. Biol.
  doi: 10.1146/annurev.cellbio.23.090506.123319
– volume: 37
  start-page: 167
  year: 2009
  end-page: 72
  ident: 133074v2.58
  article-title: ESCRTs and human disease
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0370167
– volume: 5
  start-page: 676689
  year: 2009
  ident: 133074v2.42
  article-title: In vitro reconstitution of fusion betweem immature autophagosomes and endosomes
  publication-title: Autophagy
– volume: 2
  start-page: 476
  year: 2001
  end-page: 486
  ident: 133074v2.48
  article-title: The class C Vps complex functions at multiple stages of the vacuolar transport pathway
  publication-title: Traffic.
  doi: tra020705 [pii]
– volume: 4
  start-page: 4277
  year: 2014
  ident: 133074v2.20
  article-title: Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion
  publication-title: Sci. Rep.
  doi: 10.1038/srep04277
– volume: 108
  start-page: 357
  year: 2002
  end-page: 369
  ident: 133074v2.70
  article-title: Vacuole Fusion at a Ring of Vertex Docking Sites Leaves Membrane Fragments within the Organelle
  publication-title: Cell.
– volume: 19
  start-page: 2500
  year: 2008
  end-page: 2508
  ident: 133074v2.63
  article-title: HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E08
– volume: 15
  start-page: 2593
  year: 2004
  end-page: 2605
  ident: 133074v2.65
  article-title: The Sec1/Munc18 Protein, Vps33p, Functions at the Endosome and the Vacuole of Saccharomyces cerevisiae
  publication-title: Mol. Biol. Cell.
  doi: 10.1091/mbc.E03-10-0767
– volume: 104
  start-page: 13010
  year: 2007
  end-page: 13015
  ident: 133074v2.29
  article-title: Assays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixing
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0700970104
– volume: 7
  start-page: 579
  year: 1996
  end-page: 94
  ident: 133074v2.4
  article-title: Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast
  publication-title: Mol. Biol. Cell.
– volume: 10
  start-page: 1719
  year: 1999
  end-page: 1732
  ident: 133074v2.17
  article-title: The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole
  publication-title: Mol. Biol. Cell
– volume: 104
  start-page: 8755
  year: 2007
  end-page: 8760
  ident: 133074v2.10
  article-title: Trans-SNARE complex assembly and yeast vacuole membrane fusion
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0702290104
– volume: 18
  start-page: 1072
  year: 2008
  end-page: 1077
  ident: 133074v2.5
  article-title: Osmotic Regulation of Rab-Mediated Organelle Docking
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2008.06.050
SSID ssj0002961374
Score 1.5195348
SecondaryResourceType preprint
Snippet When marked for degradation, surface receptor and transporter proteins are internalized and delivered to endosomes where they are packaged into intralumenal...
SourceID biorxiv
proquest
SourceType Open Access Repository
Aggregation Database
SubjectTerms Cell Biology
Cell fusion
Endosomes
Fusion protein
Lysosomes
SNAP receptors
Title Distinct features of multivesicular body-lysosome fusion revealed by a new cell-free content-mixing assay
URI https://www.proquest.com/docview/2071253208
https://www.biorxiv.org/content/10.1101/133074
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1NaxsxFBSN3UBO_UhMkqZGh1xFZO3Kkk6BpDEJpGYpIaQno09YiL3Orm2y_75P8ro9FHLJcdnL8nhP8zQ7zCB0LilTmnJNONec5GNoY8kyS6zixsvcOJfi2x7vxXQqn55U0RFuTSer3J2J6aB2lY0ceWRCAIszRuXl8oXE1Kj4d7WL0NhD_eiSkCXpXvGXY2EKwCoZMbOxgsFnlHfxQtCIF3A7o1Hnt2_Kqn4tN_-dxgliJp_e-3GfUb_QS19_QR_84iva34ZMtoeo_BHHeGFXOPjk4tngKuAkJNz4pkw6VGwq15Lntqmaau5xWEcODUd3J8APh02LNYb9G0ean4Taexwl7oBXZF6-AvhhWMF1e4QeJjcP17ekC1ggRrKcCDsy0mc019oF4bwZWxpk5kfC5lLTYCVXyjMLVx4nqTRamTAyInAxUoEZmw1Qb1Et_DHCsCXBqplLx7iGlSS6EArmPBdaCe64OkGDrsqz5dZFY7Yt_wk621V01k1PM_tXztO3X39DByzCLGAJE2eot6rX_jv6aDersqmHqH91My1-DVNTwFNx97P4_QdcgMFi
linkProvider ProQuest
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Nb9NAEB21KRWcgNKIQoE9lOMKZ-PN7h4QB0rUqGmUQ1SFk7WfkqUmDnYS6h_Ff2TWceBQiVsPnC1Z8r7RezOz43kAFzJhSidcU841p-kAw1iyvqVWceNlapxr7Ntux2IykfO5mh7Ar_2_MHGscs-JDVG7wsYeeeyEoBb3WSK_rH7Q6BoVb1f3Fhq7sLj29U8s2arPo0vE9yNjw2-zr1e0dRWgRrKUCtsz0mMRr7ULwnkzsEmQfd8TNpU6CVZypTyzmOc7mUijlQk9IwIXPRWYsX187SEcpRjrsgNH09HN9Pufpg5TqI7N5mc2UMg0LOGtnxFG_icsB5M4WHhs8qK8z7cP6L_RtOHz_-w0XuAp6JUvX8KBX57A8c5Es34F-WWkqaVdk-CbLaUVKQJpBiW3vsqbOVtiClfTu7oqqmLhSdjEHiGJ26tQHx0xNdEE6wsSrzFoKL0ncYQf9Zgu8nsUd4Ilhq5PYfYYH9eFzrJY-tdAMAvEVDqVjnGNKVfcsiiY81xoJbjj6gy6LajZarclJNuhfQbnewCzlh2q7C96b_79-AM8vZrdjLPxaHL9Fp6xmFKgbjJxDp11ufHv4IndrvOqfN9GIoHskdH-DY9DHck
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Distinct+features+of+multivesicular+body-lysosome+fusion+revealed+by+a+new+cell-free+content-mixing+assay&rft.jtitle=bioRxiv&rft.au=Karim%2C+Mahmoud+Abdul&rft.au=Samyn%2C+Dieter+Ronny&rft.au=Mattie%2C+Sevan&rft.au=Brett%2C+Christopher+Leonard&rft.date=2017-10-27&rft.pub=Cold+Spring+Harbor+Laboratory&rft.eissn=2692-8205&rft_id=info:doi/10.1101%2F133074&rft.externalDocID=133074v2
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2692-8205&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2692-8205&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2692-8205&client=summon