Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles.


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:
31 Oct 2023
Historique:
medline: 30 10 2023
pubmed: 26 10 2023
entrez: 26 10 2023
Statut: ppublish

Résumé

Munc13-1 is essential for vesicle docking and fusion at the active zone of synapses. Here, we report that Munc13-1 self-assembles into molecular clusters within diacylglycerol-rich microdomains present in phospholipid bilayers. Although the copy number of Munc13-1 molecules in these clusters has a broad distribution, a systematic Poisson analysis shows that this is most likely the result of two molecular species: monomers and mainly hexameric oligomers. Each oligomer is able to capture one vesicle independently. Hexamers have also been observed in crystals of Munc13-1 that form between opposed phospholipid bilayers [K. Grushin, R. V. Kalyana Sundaram, C. V. Sindelar, J. E. Rothman,

Identifiants

pubmed: 37883433
doi: 10.1073/pnas.2306086120
pmc: PMC10623011
doi:

Substances chimiques

SNARE Proteins 0
Diglycerides 0
Molecular Chaperones 0
Phospholipids 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2306086120

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK027044
Pays : United States
Organisme : NIDDK NIH HHS
ID : R37 DK027044
Pays : United States

Références

EMBO J. 2017 Mar 15;36(6):816-829
pubmed: 28137749
Proc Natl Acad Sci U S A. 2021 Mar 16;118(11):
pubmed: 33836576
Proc Natl Acad Sci U S A. 2016 Sep 20;113(38):10536-41
pubmed: 27601655
Annu Rev Biochem. 1987;56:159-93
pubmed: 3304132
Nat Struct Mol Biol. 2015 Jul;22(7):547-54
pubmed: 26030875
ACS Infect Dis. 2022 Mar 11;8(3):574-583
pubmed: 35170309
Biophys J. 1996 Nov;71(5):2623-32
pubmed: 8913600
J Gen Physiol. 2013 May;141(5):537-55
pubmed: 23630338
Neuron. 2017 Aug 2;95(3):591-607.e10
pubmed: 28772123
Proc Natl Acad Sci U S A. 2021 Feb 2;118(5):
pubmed: 33468631
J Struct Biol X. 2022 May 10;6:100068
pubmed: 35601683
J Struct Biol. 1996 Jan-Feb;116(1):71-6
pubmed: 8742726
J Cell Biol. 2020 Mar 2;219(3):
pubmed: 32211893
Elife. 2016 May 23;5:
pubmed: 27213521
J Biol Chem. 1986 Jul 5;261(19):8597-600
pubmed: 3013856
Annu Rev Biochem. 2015;84:551-75
pubmed: 25494300
Nat Commun. 2017 May 10;8:15293
pubmed: 28489077
Nat Neurosci. 2018 Jan;21(1):5-6
pubmed: 29269758
FEBS Lett. 2023 Sep;597(18):2233-2249
pubmed: 37643878
J Am Chem Soc. 2014 Mar 5;136(9):3456-64
pubmed: 24533674
Proc Natl Acad Sci U S A. 2023 Aug 22;120(34):e2309516120
pubmed: 37590407
Nat Struct Mol Biol. 2013 Jun;20(6):679-86
pubmed: 23665582
J Struct Biol. 2017 Feb;197(2):191-198
pubmed: 27313000
FEBS Lett. 2021 Feb;595(3):297-309
pubmed: 33222163
FEBS Lett. 2019 Jan;593(2):144-153
pubmed: 30561792
Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20352-7
pubmed: 21048085
Science. 2018 Aug 10;361(6402):604-607
pubmed: 29976799
FEBS Lett. 2021 Sep;595(17):2185-2196
pubmed: 34227103
Front Mol Biosci. 2022 Jun 23;9:882288
pubmed: 35813810
Biochem J. 2022 Nov 11;479(21):2311-2325
pubmed: 36367756
Proc Natl Acad Sci U S A. 2022 Feb 15;119(7):
pubmed: 35135883
Science. 2015 Dec 11;350(6266):aaa2245
pubmed: 26659058
Elife. 2017 Feb 08;6:
pubmed: 28177287
Biophys J. 2010 Jul 21;99(2):553-60
pubmed: 20643074
Nat Commun. 2020 Oct 15;11(1):5208
pubmed: 33060581
Neuron. 1998 Jul;21(1):123-36
pubmed: 9697857
Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12565-70
pubmed: 10535962
Am J Physiol. 1994 Sep;267(3 Pt 1):C659-78
pubmed: 7943196
Mol Cell. 2021 Jan 7;81(1):13-24.e7
pubmed: 33202250
Elife. 2019 Feb 28;8:
pubmed: 30816091
Nat Commun. 2019 Jan 8;10(1):69
pubmed: 30622273
Eur Biophys J. 2021 May;50(3-4):403-409
pubmed: 33651123
J Cell Biol. 2002 Sep 2;158(5):929-40
pubmed: 12213837
Nature. 1999 Jul 29;400(6743):457-61
pubmed: 10440375
Nat Neurosci. 2018 Jan;21(1):41-49
pubmed: 29230050
Nature. 2017 Aug 24;548(7668):420-425
pubmed: 28813412

Auteurs

Feng Li (F)

Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520.
Nanobiology Institute, School of Medicine, Yale University, West Haven, CT 06516.

Kirill Grushin (K)

Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520.
Nanobiology Institute, School of Medicine, Yale University, West Haven, CT 06516.

Jeff Coleman (J)

Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520.
Nanobiology Institute, School of Medicine, Yale University, West Haven, CT 06516.

Frederic Pincet (F)

Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520.
Nanobiology Institute, School of Medicine, Yale University, West Haven, CT 06516.
Laboratoire de Physique de l'Ecole normale supérieure, Département de Physique, Ecole Normale Supérieure, Université Paris Sciences & Lettres CNRS, Sorbonne Université, Université de Paris, Paris F-75005, France.

James E Rothman (JE)

Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520.
Nanobiology Institute, School of Medicine, Yale University, West Haven, CT 06516.

Articles similaires

1.00
Animals Mice Immunity, Innate Interneurons Synapses
Animals Entorhinal Cortex Interneurons Parvalbumins Mice
Humans Molecular Chaperones Brain Protein Folding Mutation
Escherichia coli Membrane Fluidity Temperature Escherichia coli Proteins Fatty Acids

Classifications MeSH