Evidence map›Paper›PMID 30955883›Full record

ArticleCell2019

The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis.

Daniel Gestaut, Soung Hun Roh, Boxue Ma, Grigore Pintilie, Lukasz A Joachimiak, Alexander Leitner, Thomas Walzthoeni, Ruedi Aebersold, Wah Chiu, Judith Frydman

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

91 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
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  8. Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  9. Calumenin prevents fibroblast senescence and lung aging by promoting vimentin proteostasis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Malaria vectors with leaky guts.Nature microbiology · 2025
    Article
  18. Article
  19. Article
  20. Article

31 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 4 countries.

Daniel GestautDepartment of Biology and Genetics, Stanford University, Stanford, CA 94305, USA.
Soung Hun RohDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Boxue MaBaylor College of Medicine, Houston, TX 77030, USA.
Grigore PintilieDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Lukasz A JoachimiakDepartment of Biology and Genetics, Stanford University, Stanford, CA 94305, USA; Department of Biochemistry, UTSouthwestern, North Campus, Dallas, TX 75390, USA.
Alexander LeitnerInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Thomas WalzthoeniInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland; PhD Program in Molecular Life Sciences, University of Zurich/ETH Zurich, 8057 Zurich, Switzerland; Institute of Computational Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
Ruedi AebersoldInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland; Faculty of Science, University of Zurich, Zurich, Switzerland.
Wah ChiuDepartment of Bioengineering, Stanford University, Stanford, CA 94305, USA.
Judith FrydmanDepartment of Biology and Genetics, Stanford University, Stanford, CA 94305, USA. Electronic address: jfrydman@stanford.edu.
Stanford University · USSeoul National University · KRUniversity of Zurich · CHBaylor College of Medicine · USETH Zurich · CH

Funding

The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
Mechanism of the Eukaryotic Chaperonin TRiC/CCTR01GM074074 · NIGMS · STANFORD UNIVERSITY · PI FRYDMAN, JUDITH · 2005 to 2024
$6.8M
Project 3: TRiC modulation of CNS pathogenesis in HD mouse modelsP01NS092525 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI THOMPSON, LESLIE MICHELS · 2016 to 2020
$6.3M
Mechanisms of the eukaryotic chaperonin TRiC/CCT and its cochaperone PrefoldinF32GM103124 · NIGMS · STANFORD UNIVERSITY · PI GESTAUT, DAN · 2012 to 2014
$156k
NIGMS NIH HHS F32 GM103124NIGMS NIH HHS P41 GM103832NIGMS NIH HHS R01 GM074074NIGMS NIH HHS R01 GM079429NINDS NIH HHS P01 NS092525
6 · The paper itself

Abstract

Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis.

Indexed as

ActinsChaperonin Containing TCP-1Cryoelectron MicroscopyHumansModels, MolecularMolecular ChaperonesProtein FoldingProtein Structure, QuaternaryProtein SubunitsProteostasisRecombinant ProteinsSaccharomyces cerevisiaeStatic ElectricityActinsChaperonin Containing TCP-1Molecular ChaperonesprefoldinProtein SubunitsRecombinant ProteinsCCTchaperonechaperonincryo-EMGIMcprefoldinproteostasisTRiCXL-MS

Identifiers

PMID30955883
PMCPMC6629582
OpenAlexW2929944850

What OpenQuestion holds

Textmetadata
LicenceTDM
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.