Evidence map›Paper›PMID 28112172›Full record

ArticleNature communications2017

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

Peng Yue, Yubo Zhang, Kunrong Mei, Shaoxiao Wang, Johannes Lesigang, Yueyao Zhu, Gang Dong, Wei Guo

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  7. The exocyst in context.Biochemical Society transactions · 2024
    Review
  8. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
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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

8 authors.

Peng YueDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Yubo ZhangDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Kunrong MeiDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Shaoxiao WangDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Johannes LesigangDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Yueyao ZhuDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Gang DongDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Wei GuoDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Funding

Molecular Regulation of ExocytosisR01GM111128 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GUO, WEI · 2014 to 2020
$2.4M
Austrian Science Fund FWF P 23440NIGMS NIH HHS R01 GM111128
6 · The paper itself

Abstract

The soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) constitute the core machinery for membrane fusion during eukaryotic cell vesicular trafficking. However, how the assembly of the SNARE complex is initiated is unknown. Here we report that Sec3, a component of the exocyst complex that mediates vesicle tethering during exocytosis, directly interacts with the t-SNARE protein Sso2. This interaction promotes the formation of an Sso2-Sec9 'binary' t-SNARE complex, the early rate-limiting step in SNARE complex assembly, and stimulates membrane fusion. The crystal structure of the Sec3-Sso2 complex suggests that Sec3 binding induces conformational changes of Sso2 that are crucial for the relief of its auto-inhibition. Interestingly, specific disruption of the Sec3-Sso2 interaction in cells blocks exocytosis without affecting the function of Sec3 in vesicle tethering. Our study reveals an activation mechanism for SNARE complex assembly, and uncovers a role of the exocyst in promoting membrane fusion in addition to vesicle tethering.

Indexed as

Cell ExtractsCell MembraneCrystallizationGene Expression RegulationGene Expression Regulation, FungalLiposomesMembrane FusionModels, MolecularProtein BindingProtein ConformationQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsCell ExtractsLiposomesQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC3 protein, S cerevisiaeSNARE ProteinsSSO1 protein, S cerevisiaeSSO2 protein, S cerevisiae

Identifiers

PMID28112172
PMCPMC5267525

What OpenQuestion holds

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Registered trials

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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.