Evidence map›Paper›PMID 26473735›Full record

ArticlePLoS genetics2015

Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.

Navinder Kumar, Deepika Gaur, Arpit Gupta, Anuradhika Puri, Deepak Sharma

Abstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020
    Review
  7. Article
  8. Review
  9. Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases.International journal of molecular sciences · 2019
    Review
  10. Review
  11. Review
  12. Review
  13. Genetics · 2018
    Article
  14. Article
  15. Article
  16. Microbial cyclophilins: specialized functions in virulence and beyond.World journal of microbiology & biotechnology · 2017
    Review
  17. Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  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

5 authors.

Navinder KumarCouncil of Scientific and Industrial Research-Institute of Microbial Technology, Chandigarh, India.
Deepika GaurCouncil of Scientific and Industrial Research-Institute of Microbial Technology, Chandigarh, India.
Arpit GuptaCouncil of Scientific and Industrial Research-Institute of Microbial Technology, Chandigarh, India.
Anuradhika PuriCouncil of Scientific and Industrial Research-Institute of Microbial Technology, Chandigarh, India.
Deepak SharmaCouncil of Scientific and Industrial Research-Institute of Microbial Technology, Chandigarh, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of Hsp70 chaperones in yeast prion propagation is well established. Highly conserved Hsp90 chaperones participate in a number of cellular processes, such as client protein maturation, protein degradation, cellular signalling and apoptosis, but little is known about their role in propagation of infectious prion like aggregates. Here, we examine the influence of Hsp90 in the maintenance of yeast prion [URE3] which is a prion form of native protein Ure2, and reveal a previously unknown role of Hsp90 as an important regulator of [URE3] stability. We show that the C-terminal MEEVD pentapeptide motif, but not the client maturation activity of Hsp90, is essential for [URE3] prion stability. In testing deletions of various Hsp90 co-chaperones known to bind this motif, we find the immunophilin homolog Cpr7 is essential for [URE3] propagation. We show that Cpr7 interacts with Ure2 and enhances its fibrillation. The requirement of Cpr7 is specific for [URE3] as its deletion does not antagonize both strong and weak variant of another yeast prion [PSI+], suggesting a distinct role of the Hsp90 co-chaperone with different yeast prions. Our data show that, similar to the Hsp70 family, the Hsp90 chaperones also influence yeast prion maintenance, and that immunophilins could regulate protein multimerization independently of their activity as peptidyl-prolyl isomerases.

Indexed as

Amino Acid MotifsCyclophilinsGlutathione PeroxidaseHSP90 Heat-Shock ProteinsMitosisMolecular ChaperonesPeptidyl-Prolyl Isomerase DPeptidyl-Prolyl Isomerase FPrionsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCPR7 protein, S cerevisiaeCyclophilinsGlutathione PeroxidaseHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMolecular ChaperonesPeptidyl-Prolyl Isomerase DPeptidyl-Prolyl Isomerase FPrionsSaccharomyces cerevisiae ProteinsURE2 protein, S cerevisiae

Identifiers

PMID26473735
PMCPMC4608684

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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.