Evidence map›Paper›PMID 27253060›Full record

ArticleeLife2016

Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex.

Ucheor B Choi, Minglei Zhao, Yunxiang Zhang, Ying Lai, Axel T Brunger

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.7field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. The pre-synaptic fusion machinery.Current opinion in structural biology · 2019
    Review
  17. Article
  18. CaTrends in cell biology · 2018
    Review
  19. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ucheor B ChoiDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, United States.
Minglei ZhaoDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, United States.
Yunxiang ZhangDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, United States.
Ying LaiDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, United States.
Axel T BrungerDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, United States.ORCID 0000-0001-5121-2036
Howard Hughes Medical Institute · US

Funding

Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Howard Hughes Medical InstituteNIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

Complexin regulates spontaneous and activates Ca(2+)-triggered neurotransmitter release, yet the molecular mechanisms are still unclear. Here we performed single molecule fluorescence resonance energy transfer experiments and uncovered two conformations of complexin-1 bound to the ternary SNARE complex. In the cis conformation, complexin-1 induces a conformational change at the membrane-proximal C-terminal end of the ternary SNARE complex that specifically depends on the N-terminal, accessory, and central domains of complexin-1. The complexin-1 induced conformation of the ternary SNARE complex may be related to a conformation that is juxtaposing the synaptic vesicle and plasma membranes. In the trans conformation, complexin-1 can simultaneously interact with a ternary SNARE complex via the central domain and a binary SNARE complex consisting of syntaxin-1A and SNAP-25A via the accessory domain. The cis conformation may be involved in activation of synchronous neurotransmitter release, whereas both conformations may be involved in regulating spontaneous release.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsCell MembraneFluorescence Resonance Energy TransferNerve Tissue ProteinsProtein BindingProtein ConformationRatsSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1Adaptor Proteins, Vesicular Transportcomplexin INerve Tissue ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1biophysicscalcium triggeringneuroscienceneurotransmitter releaseratstructural biologysynaptic vesicle fusion

Identifiers

PMID27253060
PMCPMC4927292
OpenAlexW2411541314

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.