Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.
Adenosine Triphosphatases
/ physiology
Endoplasmic Reticulum
/ metabolism
Golgi Apparatus
/ metabolism
Intracellular Membranes
/ physiology
Lysosomes
/ metabolism
Membrane Fusion
/ physiology
Molecular Chaperones
/ physiology
Multiprotein Complexes
Munc18 Proteins
/ metabolism
Organ Specificity
Organelles
/ metabolism
Proteolipids
/ metabolism
Recombinant Proteins
/ metabolism
SNARE Proteins
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ physiology
Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
/ physiology
Vacuoles
/ metabolism
Vesicular Transport Proteins
/ physiology
NSF
SM protein
SNARE
membrane fusion
α-SNAP
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
19 11 2019
19 11 2019
Historique:
pubmed:
7
11
2019
medline:
21
4
2020
entrez:
6
11
2019
Statut:
ppublish
Résumé
Membrane fusion at each organelle requires conserved proteins: Rab-GTPases, effector tethering complexes, Sec1/Munc18 (SM)-family SNARE chaperones, SNAREs of the R, Qa, Qb, and Qc families, and the Sec17/α-SNAP and ATP-dependent Sec18/NSF SNARE chaperone system. The basis of organelle-specific fusion, which is essential for accurate protein compartmentation, has been elusive. Rab family GTPases, SM proteins, and R- and Q-SNAREs may contribute to this specificity. We now report that the fusion supported by SNAREs alone is both inefficient and promiscuous with respect to organelle identity and to stimulation by SM family proteins or complexes. SNARE-only fusion is abolished by the disassembly chaperones Sec17 and Sec18. Efficient fusion in the presence of Sec17 and Sec18 requires a tripartite match between the organellar identities of the R-SNARE, the Q-SNAREs, and the SM protein or complex. The functions of Sec17 and Sec18 are not simply negative regulation; they stimulate fusion with either vacuolar SNAREs and their SM protein complex HOPS or endoplasmic reticulum/
Identifiants
pubmed: 31685636
pii: 1913985116
doi: 10.1073/pnas.1913985116
pmc: PMC6876204
doi:
Substances chimiques
Molecular Chaperones
0
Multiprotein Complexes
0
Munc18 Proteins
0
Proteolipids
0
Recombinant Proteins
0
SEC17 protein, S cerevisiae
0
SNARE Proteins
0
Saccharomyces cerevisiae Proteins
0
Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
0
Vesicular Transport Proteins
0
proteoliposomes
0
Adenosine Triphosphatases
EC 3.6.1.-
SEC18 protein, S cerevisiae
EC 3.6.1.-
Types de publication
Comparative Study
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
23573-23581Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118037
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing interest.
Références
Mol Biol Cell. 2010 Jul 1;21(13):2297-305
pubmed: 20462954
Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2701-6
pubmed: 16469845
Mol Biol Cell. 2015 Jan 15;26(2):305-15
pubmed: 25411340
Mol Biol Cell. 2017 Mar 15;28(6):707-711
pubmed: 28292915
Elife. 2017 Jul 18;6:
pubmed: 28718762
Biophys J. 2006 Mar 1;90(5):1661-75
pubmed: 16339880
Cell. 2003 Feb 21;112(4):519-33
pubmed: 12600315
Nat Commun. 2019 Apr 8;10(1):1608
pubmed: 30962439
Nature. 2017 Nov 30;551(7682):634-638
pubmed: 29088698
Nature. 2000 Sep 14;407(6801):153-9
pubmed: 11001046
J Cell Biol. 2009 May 4;185(3):535-49
pubmed: 19414611
EMBO J. 2008 Aug 6;27(15):2031-42
pubmed: 18650938
J Am Chem Soc. 2015 Oct 14;137(40):12873-83
pubmed: 26431309
Proc Natl Acad Sci U S A. 2015 May 5;112(18):E2290-7
pubmed: 25902545
J Cell Biol. 2002 Apr 1;157(1):45-62
pubmed: 11927603
J Cell Biol. 1997 Aug 11;138(3):517-29
pubmed: 9245783
Mol Biol Cell. 2017 Apr 1;28(7):975-983
pubmed: 28148647
Annu Rev Cell Dev Biol. 2010;26:115-36
pubmed: 20521906
J Cell Biol. 2008 Sep 22;182(6):1141-51
pubmed: 18809726
Science. 2015 Sep 4;349(6252):1111-4
pubmed: 26339030
J Biol Chem. 2018 Jan 26;293(4):1346-1352
pubmed: 29208657
Nature. 1997 May 8;387(6629):199-202
pubmed: 9144293
Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9402-7
pubmed: 10944212
Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11821-7
pubmed: 16882731
EMBO J. 2006 Apr 19;25(8):1579-89
pubmed: 16601699
J Biol Chem. 1992 Sep 15;267(26):18665-70
pubmed: 1526998
EMBO J. 2010 Jun 16;29(12):1948-60
pubmed: 20473271
J Cell Biol. 1996 Mar;132(5):787-94
pubmed: 8603912
Sci Rep. 2014 Mar 04;4:4277
pubmed: 24589832
Annu Rev Cell Dev Biol. 2010;26:137-56
pubmed: 19575650
Mol Biol Cell. 2017 Jan 15;28(2):322-332
pubmed: 27852901
Elife. 2018 Dec 12;7:
pubmed: 30540253
J Cell Biol. 2004 Dec 20;167(6):1087-98
pubmed: 15611334
Nat Rev Mol Cell Biol. 2016 Aug;17(8):465-79
pubmed: 27301672
Elife. 2014 Jan 01;3:e01879
pubmed: 24596153
Annu Rev Cell Dev Biol. 2012;28:279-308
pubmed: 23057743
Cold Spring Harb Perspect Biol. 2011 Jul 01;3(7):null
pubmed: 21482742
J Biol Chem. 2013 Oct 4;288(40):28557-66
pubmed: 23955338
Neuron. 2017 Aug 2;95(3):591-607.e10
pubmed: 28772123
J Biol Chem. 1999 Feb 26;274(9):5649-53
pubmed: 10026182
Mol Biol Cell. 2011 Dec;22(23):4635-46
pubmed: 21976702
Elife. 2014 Sep 25;3:e03251
pubmed: 25255215
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15781-6
pubmed: 9861047
Front Cell Dev Biol. 2016 Mar 30;4:20
pubmed: 27066478
J Biol Chem. 1999 May 28;274(22):15440-6
pubmed: 10336434
Proc Natl Acad Sci U S A. 2019 Jul 9;116(28):13952-13957
pubmed: 31235584
Traffic. 2004 Jan;5(1):45-52
pubmed: 14675424
Nature. 2015 Feb 5;518(7537):61-7
pubmed: 25581794