Evidence map›Paper›PMID 32239688›Full record

ArticleProtein science : a publication of the Protein Society2020

Integrative structure and function of the yeast exocyst complex.

Sai J Ganesan, Michael J Feyder, Ilan E Chemmama, Fei Fang, Michael P Rout, Brian T Chait, Yi Shi, Mary Munson, Andrej Sali

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  4. Review
  5. Article
  6. Article
  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. Review
  10. Article
  11. Article
  12. Modeling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

9 authors at 4 institutions in 1 country.

Sai J GanesanDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.ORCID 0000-0002-8335-2866
Michael J FeyderDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.ORCID 0000-0001-5233-6161
Ilan E ChemmamaDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.ORCID 0000-0002-5657-3516
Fei FangDepartment of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Michael P RoutLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York, USA.ORCID 0000-0003-2010-706X
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York, USA.ORCID 0000-0003-3524-557X
Yi ShiDepartment of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Mary MunsonDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.ORCID 0000-0003-2297-8053
Andrej SaliDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.ORCID 0000-0003-0435-6197
University of California, San Francisco · USRockefeller University · USUniversity of Massachusetts Chan Medical School · USUniversity of Pittsburgh · US

Funding

TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
Structure-Function Mapping of the Nuclear Pore Complex-RenewalR01GM112108 · NIGMS · ROCKEFELLER UNIVERSITY · PI JOHN D. AITCHISON, MICHAEL P ROUT · 2015 to 2026
$9.1M
Structure and Function of the Exocyst ComplexR01GM068803 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNSON, MARY · 2005 to 2021
$7.4M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
High Performance Computer for Computational BiosciencesS10OD021596 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2016 to 2016
$443k
NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM068803NIGMS NIH HHS R01 GM083960NIGMS NIH HHS R01 GM112108NIGMS NIH HHS T32 GM008284NIH HHS GM068803NIH HHS GM103314NIH HHS P41 GM109824NIH HHS R01GM083960NIH HHS R01 GM112108NIH HHS S10 OD021596
6 · The paper itself

Abstract

Exocyst is an evolutionarily conserved hetero-octameric tethering complex that plays a variety of roles in membrane trafficking, including exocytosis, endocytosis, autophagy, cell polarization, cytokinesis, pathogen invasion, and metastasis. Exocyst serves as a platform for interactions between the Rab, Rho, and Ral small GTPases, SNARE proteins, and Sec1/Munc18 regulators that coordinate spatial and temporal fidelity of membrane fusion. However, its mechanism is poorly described at the molecular level. Here, we determine the molecular architecture of the yeast exocyst complex by an integrative approach, based on a 3D density map from negative-stain electron microscopy (EM) at ~16 Å resolution, 434 disuccinimidyl suberate and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride cross-links from chemical-crosslinking mass spectrometry, and partial atomic models of the eight subunits. The integrative structure is validated by a previously determined cryo-EM structure, cross-links, and distances from in vivo fluorescence microscopy. Our subunit configuration is consistent with the cryo-EM structure, except for Sec5. While not observed in the cryo-EM map, the integrative model localizes the N-terminal half of Sec3 near the Sec6 subunit. Limited proteolysis experiments suggest that the conformation of Exo70 is dynamic, which may have functional implications for SNARE and membrane interactions. This study illustrates how integrative modeling based on varied low-resolution structural data can inform biologically relevant hypotheses, even in the absence of high-resolution data.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayModels, MolecularProtein ConformationProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein SubunitsSaccharomyces cerevisiae Proteinschemical cross-linking mass spectrometryEMexocytosisintegrative modelingmembrane fusionprotein cross-linkingSNAREsstructural modelsyeast exocyst complex

Identifiers

PMID32239688
PMCPMC7255525
OpenAlexW3014106448

What OpenQuestion holds

Textmetadata
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.