Evidence map›Paper›PMID 31253771›Full record

ArticleNature communications2019

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly.

Jorge Cuéllar, W Grant Ludlam, Nicole C Tensmeyer, Takuma Aoba, Madhura Dhavale, César Santiago, M Teresa Bueno-Carrasco, Michael J Mann, Rebecca L Plimpton, Aman Makaju and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structures of the 26Science advances · 2026
    Article
  5. Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  6. Article
  7. Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  8. Article
  9. Methods to Study CCT Expression and Impact on Cytoskeleton.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. The Open Conformation of CCT: How to Achieve High Resolution Using CryoEM.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  11. CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  17. Review
  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

13 authors at 4 institutions in 2 countries.

Jorge CuéllarCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
W Grant LudlamDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.ORCID http://orcid.org/0000-0002-2701-8791
Nicole C TensmeyerDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.ORCID http://orcid.org/0000-0003-4957-7129
Takuma AobaDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
Madhura DhavaleDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
César SantiagoCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
M Teresa Bueno-CarrascoCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain.
Michael J MannDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
Rebecca L PlimptonDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA.
Aman MakajuDepartment of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah, Salt Lake City, UT, 84112, USA.
Sarah FranklinDepartment of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah, Salt Lake City, UT, 84112, USA.
Barry M WillardsonDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, 84602, USA. bmwillardson@chem.byu.edu.
José M ValpuestaCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, 28049, Madrid, Spain. jmv@cnb.csic.es.ORCID http://orcid.org/0000-0001-7468-8053
Brigham Young University · USCentro Nacional de Biotecnología · ESUniversidad Autónoma de Madrid · ESUniversity of Utah · US

Funding

Structural basis for chaperone-dependent folding of beta-propeller proteins essential for visionR01EY012287 · NEI · BRIGHAM YOUNG UNIVERSITY · PI WILLARDSON, BARRY M · 1999 to 2022
$5.7M
NEI NIH HHS R01 EY012287U.S. Department of Health & Human Services | National Institutes of Health (NIH) EY012287
6 · The paper itself

Abstract

The mechanistic target of rapamycin (mTOR) kinase forms two multi-protein signaling complexes, mTORC1 and mTORC2, which are master regulators of cell growth, metabolism, survival and autophagy. Two of the subunits of these complexes are mLST8 and Raptor, β-propeller proteins that stabilize the mTOR kinase and recruit substrates, respectively. Here we report that the eukaryotic chaperonin CCT plays a key role in mTORC assembly and signaling by folding both mLST8 and Raptor. A high resolution (4.0 Å) cryo-EM structure of the human mLST8-CCT intermediate isolated directly from cells shows mLST8 in a near-native state bound to CCT deep within the folding chamber between the two CCT rings, and interacting mainly with the disordered N- and C-termini of specific CCT subunits of both rings. These findings describe a unique function of CCT in mTORC assembly and a distinct binding site in CCT for mLST8, far from those found for similar β-propeller proteins.

Indexed as

Amino Acid SequenceBinding SitesChaperonin Containing TCP-1Cryoelectron MicroscopyGene Expression RegulationGene Knockdown TechniquesHEK293 CellsHep G2 CellsHumansMass SpectrometryModels, MolecularmTOR Associated Protein, LST8 HomologProtein BindingProtein ConformationProtein FoldingRegulatory-Associated Protein of mTORChaperonin Containing TCP-1MLST8 protein, humanmTOR Associated Protein, LST8 HomologMTOR protein, humanRegulatory-Associated Protein of mTORRPTOR protein, humanTOR Serine-Threonine Kinases

Identifiers

PMID31253771
PMCPMC6599039
OpenAlexW2953614388

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.