Evidence map›Paper›PMID 29170376›Full record

ArticleNature communications2017

Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.

Manikandan Karuppasamy, Beata Kusmider, Taiana M Oliveira, Christl Gaubitz, Manoel Prouteau, Robbie Loewith, Christiane Schaffitzel

Open access · goldAbstract 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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.6field-weighted citation impact, top 6% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  4. Review
  5. Sample Preparation for Electron Cryo-Microscopy of Macromolecular Machines.Advances in experimental medicine and biology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. The central moTOR of metabolism.Developmental cell · 2022
    Review
  10. RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Review
  12. Article
  13. Ras, PI3K and mTORC2 - three's a crowd?Journal of cell science · 2020
    Review
  14. Review
  15. Review
  16. The Importance of TOR Kinase in Plant Development.Frontiers in plant science · 2020
    Review
  17. Article
  18. Targeting mTOR for cancer therapy.Journal of hematology & oncology · 2019
    Review
  19. Article
  20. Analysis of the roles of phosphatidylinositol-4,5-Molecular biology of the cell · 2019
    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

7 authors at 3 institutions in 3 countries.

Manikandan KaruppasamyEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042, Grenoble, France.
Beata KusmiderDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, 30 Quai Ernest Ansermet, CH1211, Geneva, Switzerland.
Taiana M OliveiraEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042, Grenoble, France.
Christl GaubitzDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, 30 Quai Ernest Ansermet, CH1211, Geneva, Switzerland.
Manoel ProuteauDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, 30 Quai Ernest Ansermet, CH1211, Geneva, Switzerland.
Robbie LoewithDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, 30 Quai Ernest Ansermet, CH1211, Geneva, Switzerland. robbie.loewith@unige.ch.
Christiane SchaffitzelEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042, Grenoble, France. christiane.berger-schaffitzel@bristol.ac.uk.ORCID http://orcid.org/0000-0002-1516-9760
University of Geneva · CHEuropean Molecular Biology Laboratory · FRUniversity of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes. Avo3/Rictor is unique to TORC2, but interacts with the same HEAT repeats of Tor2 that are engaged by Kog1/Raptor in mammalian TORC1, explaining the mutual exclusivity of these two proteins. Density, which we conclude is Avo3, occludes the FKBP12-rapamycin-binding site of Tor2's FRB domain rendering TORC2 rapamycin insensitive and recessing the kinase active site. Although mobile, Avo1/hSin1 further restricts access to the active site as its conserved-region-in-the-middle (CRIM) domain is positioned along an edge of the TORC2 active-site-cleft, consistent with a role for CRIM in substrate recruitment.

Indexed as

Binding SitesCarrier ProteinsCryoelectron MicroscopyMechanistic Target of Rapamycin Complex 2Models, MolecularProtein Interaction Domains and MotifsProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAvo1 protein, S cerevisiaeCarrier ProteinsMechanistic Target of Rapamycin Complex 2Saccharomyces cerevisiae ProteinsTORC1 protein complex, S cerevisiaeTranscription FactorsTSC11 protein, S cerevisiae

Identifiers

PMID29170376
PMCPMC5700991
OpenAlexW2768854532

What OpenQuestion holds

Textmetadata
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.