Evidence map›Paper›PMID 29335562›Full record

ArticleNature structural & molecular biology2018

Cryo-EM structure of the exocyst complex.

Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang, Yuehe Ding, Guangzuo Luo, Peng Yue, Jun-Jie Liu, Xinquan Wang and 3 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing 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

91 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
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  12. Preassembly and independent trafficking of the exocyst complex inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. The exocyst in ciliogenesis.Renal failure · 2025
    Review
  15. Article
  16. Article
  17. The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
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31 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Kunrong MeiDepartment of Biology, University of Pennsylvania, Philadelphia, PA, USA.
Yan LiMinistry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
Shaoxiao WangDepartment of Biology, University of Pennsylvania, Philadelphia, PA, USA.
Guangcan ShaoNational Institute of Biological Sciences, Beijing, China.
Jia WangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
Yuehe DingNational Institute of Biological Sciences, Beijing, China.
Guangzuo LuoDepartment of Biology, University of Pennsylvania, Philadelphia, PA, USA.
Peng YueDepartment of Biology, University of Pennsylvania, Philadelphia, PA, USA.
Jun-Jie LiuMinistry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
Xinquan WangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-6094-1182
Hong-Wei WangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China. hongweiwang@tsinghua.edu.cn.
Wei GuoDepartment of Biology, University of Pennsylvania, Philadelphia, PA, USA. guowei@sas.upenn.edu.ORCID http://orcid.org/0000-0002-9251-0360
Tsinghua University · CNUniversity of Pennsylvania · USNational Institute of Biological Sciences, Beijing · CN

Funding

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

Abstract

The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the structure of the Saccharomyces cerevisiae exocyst complex at an average resolution of 4.4 Å. Our model revealed the architecture of the exocyst and led to the identification of the helical bundles that mediate the assembly of the complex at its core. Sequence analysis suggests that these regions are evolutionarily conserved across eukaryotic systems. Additional cell biological data suggest a mechanism for exocyst assembly that leads to vesicle tethering at the plasma membrane.

Indexed as

ExocytosisAmino Acid MotifsBiological TransportCell MembraneCross-Linking ReagentsCryoelectron MicroscopyCytoplasmGolgi ApparatusImage Processing, Computer-AssistedMass SpectrometryProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVesicular Transport ProteinsCross-Linking ReagentsSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID29335562
PMCPMC5971111
OpenAlexW2783965229

What OpenQuestion holds

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LicenceTDM
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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.