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  Morphologies of synaptic protein membrane fusion interfaces

Gipson, P., Fukuda, Y., Danev, R., Lai, Y., Chen, D.-H., Baumeister, W., et al. (2017). Morphologies of synaptic protein membrane fusion interfaces. Proceedings of the National Academy of Sciences of the United States of America, 114(34), 9110-9115. doi:10.1073/pnas.1708492114.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E24F-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E250-9
Genre: Journal Article

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PNAS-2017-Gipson-9110-5.pdf (Publisher version), 5MB
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 Creators:
Gipson, Preeti1, Author
Fukuda, Yoshiyuki2, Author              
Danev, Radostin2, Author              
Lai, Ying1, Author
Chen, Dong-Hua1, Author
Baumeister, Wolfgang2, Author              
Brunger, Axel T.1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: NEUROTRANSMITTER RELEASE; CRYOELECTRON TOMOGRAPHY; 3-DIMENSIONAL STRUCTURE; PHASE PLATE; SNARE; COMPLEX; VESICLE; VISUALIZATION; ARCHITECTURE; EXOCYTOSISScience & Technology - Other Topics; synaptic vesicle fusion; neurotransmitter release; Volta phase plate; electron cryotomography; Munc13;
 Abstract: Neurotransmitter release is orchestrated by synaptic proteins, such as SNAREs, synaptotagmin, and complexin, but the molecular mechanisms remain unclear. We visualized functionally active synaptic proteins reconstituted into proteoliposomes and their interactions in a native membrane environment by electron cryotomography with a Volta phase plate for improved resolvability. The images revealed individual synaptic proteins and synaptic protein complex densities at prefusion contact sites between membranes. We observed distinct morphologies of individual synaptic proteins and their complexes. The minimal system, consisting of neuronal SNAREs and synaptotagmin-1, produced point and long-contact prefusion states. Morphologies and populations of these states changed as the regulatory factors complexin and Munc13 were added. Complexin increased the membrane separation, along with a higher propensity of point contacts. Further inclusion of the priming factor Munc13 exclusively restricted prefusion states to point contacts, all of which efficiently fused upon Ca2+ triggering. We conclude that synaptic proteins have evolved to limit possible contact site assemblies and morphologies to those that promote fast Ca2+-triggered release.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000408095300062
DOI: 10.1073/pnas.1708492114
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (34) Sequence Number: - Start / End Page: 9110 - 9115 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230