Evidence map›Paper›PMID 30911017›Full record

ArticleScientific reports2019

The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism.

Lucía Quintana-Gallardo, Jaime Martín-Benito, Miguel Marcilla, Guadalupe Espadas, Eduard Sabidó, José María Valpuesta

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Hsp90: A means to an end.Cell stress & chaperones · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Structures of the 26Science advances · 2026
    Article
  8. Review
  9. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Chaperone Proteins: The Rising Players in Muscle Atrophy.Journal of cachexia, sarcopenia and muscle · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. 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

6 authors at 2 institutions in 1 country.

Lucía Quintana-GallardoCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.
Jaime Martín-BenitoCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.ORCID http://orcid.org/0000-0002-8541-4709
Miguel MarcillaCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.ORCID http://orcid.org/0000-0001-9171-5076
Guadalupe EspadasProteomics Unit, Centre de Regulació Genòmica (CRG), Barcelona Institute of Science and Technology (BIST), Barcelona, Spain.
Eduard SabidóProteomics Unit, Centre de Regulació Genòmica (CRG), Barcelona Institute of Science and Technology (BIST), Barcelona, Spain.ORCID http://orcid.org/0000-0001-6506-7714
José María ValpuestaCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049, Madrid, Spain. jmv@cnb.csic.es.ORCID http://orcid.org/0000-0001-7468-8053
Centro Nacional de Biotecnología · ESUniversitat Pompeu Fabra · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case for Hsp70 and Hsp90 which, in concert with the cochaperone CHIP, direct their bound substrate to degradation through ubiquitination. We generated complexes between the chaperones (Hsp70 or Hsp90), the cochaperone CHIP and, as substrate, a p53 variant containing the GST protein (p53-TMGST). Both ternary complexes (Hsp70:p53-TMGST:CHIP and Hsp90:p53-TMGST:CHIP) ubiquitinated the substrate at a higher efficiency than in the absence of the chaperones. The 3D structures of the two complexes, obtained using a combination of cryoelectron microscopy and crosslinking mass spectrometry, showed the substrate located between the chaperone and the cochaperone, suggesting a ubiquitination mechanism in which the chaperone-bound substrate is presented to CHIP. These complexes are inherently flexible, which is important for the ubiquitination process.

Indexed as

Chromatography, GelChromatography, LiquidCryoelectron MicroscopyHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMass SpectrometryMicroscopy, Electron, TransmissionMolecular ChaperonesProtein FoldingTandem Mass SpectrometryUbiquitinationHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID30911017
PMCPMC6433865
OpenAlexW2925078176

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.