Evidence map›Paper›PMID 35449234›Full record

ArticleNature structural & molecular biology2022

Snapshots of actin and tubulin folding inside the TRiC chaperonin.

John J Kelly, Dale Tranter, Els Pardon, Gamma Chi, Holger Kramer, Lotta Happonen, Kelly M Knee, Jay M Janz, Jan Steyaert, Christine Bulawa and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Alterations of actin in aging.Journal of cell science · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  13. Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  18. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  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 7 institutions in 5 countries.

John J KellyCentre for Medicines Discovery, Nuffield Department of Clinical Medicine, University of Oxford, Oxford, UK.
Dale TranterInstitute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland.
Els PardonStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID http://orcid.org/0000-0002-2466-0172
Gamma ChiCentre for Medicines Discovery, Nuffield Department of Clinical Medicine, University of Oxford, Oxford, UK.
Holger KramerBiological Mass Spectrometry and Proteomics Facility, MRC London Institute of Medical Sciences, Imperial College London, Hammersmith Hospital Campus, London, UK.ORCID http://orcid.org/0000-0002-6400-0945
Lotta HapponenDivision of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden.ORCID http://orcid.org/0000-0002-5922-4549
Kelly M KneePfizer Rare Disease Research Unit, Worldwide Research and Development, Pfizer Inc., Cambridge, MA, USA.
Jay M JanzPfizer Rare Disease Research Unit, Worldwide Research and Development, Pfizer Inc., Cambridge, MA, USA.
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID http://orcid.org/0000-0002-3825-874X
Christine BulawaPfizer Rare Disease Research Unit, Worldwide Research and Development, Pfizer Inc., Cambridge, MA, USA.
Ville O PaavilainenInstitute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-3160-7767
Juha T HuiskonenInstitute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland. juha.huiskonen@helsinki.fi.ORCID http://orcid.org/0000-0002-0348-7323
Wyatt W YueCentre for Medicines Discovery, Nuffield Department of Clinical Medicine, University of Oxford, Oxford, UK. wyatt.yue@cmd.ox.ac.uk.ORCID http://orcid.org/0000-0001-6959-6007
Pfizer (United States) · USUniversity of Oxford · GBUniversity of Helsinki · FIVrije Universiteit Brussel · BECentre for Human Genetics · GBHammersmith Hospital · GBLund University · SE

Funding

Medical Research Council MC_PC_17137Wellcome TrustWellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC.

Indexed as

ActinsTubulinChaperonin Containing TCP-1ChaperoninsHumansMalePeptidesProtein FoldingActinsChaperonin Containing TCP-1ChaperoninsPeptidesTubulin

Identifiers

PMID35449234
PMCPMC9113939
OpenAlexW4226140689

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.