Evidence map›Paper›PMID 25329162›Full record

ArticlePLoS genetics2014

Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.

Michael Reidy, Ruchika Sharma, Shankar Shastry, Brittany-Lee Roberts, Ivan Albino-Flores, Sue Wickner, Daniel C Masison

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 64 citations in OpenAlex.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  10. Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Differential Thermotolerance Adaptation between Species ofJournal of fungi (Basel, Switzerland) · 2020
    Article
  15. Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020
    Review
  17. 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

7 authors at 3 institutions in 1 country.

Michael ReidyLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, United States of America.
Ruchika SharmaLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, United States of America.
Shankar ShastryLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
Brittany-Lee RobertsLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, United States of America.
Ivan Albino-FloresLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, United States of America.
Sue WicknerLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
Daniel C MasisonLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, United States of America.
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Cancer Institute · USNational Institutes of Health · US

Funding

Molecular Chaperones and DNA ReplicationZIABC008710 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WICKNER, SUE H · 2009 to 2025
$24.5M
Yeast prions and Hsp70 co-chaperonesZIADK024952 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MASISON, DANIEL · 2009 to 2015
$2.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Hsp100 family chaperones of microorganisms and plants cooperate with the Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast this machinery also promotes propagation of prions by fragmenting prion polymers. We previously showed the bacterial Hsp100 machinery cooperates with the yeast Hsp40 Ydj1 to support yeast thermotolerance and with the yeast Hsp40 Sis1 to propagate [PSI+] prions. Here we find these Hsp40s similarly directed specific activities of the yeast Hsp104-based machinery. By assessing the ability of Ydj1-Sis1 hybrid proteins to complement Ydj1 and Sis1 functions we show their C-terminal substrate-binding domains determined distinctions in these and other cellular functions of Ydj1 and Sis1. We find propagation of [URE3] prions was acutely sensitive to alterations in Sis1 activity, while that of [PIN+] prions was less sensitive than [URE3], but more sensitive than [PSI+]. These findings support the ideas that overexpressing Ydj1 cures [URE3] by competing with Sis1 for interaction with the Hsp104-based disaggregation machine, and that different prions rely differently on activity of this machinery, which can explain the various ways they respond to alterations in chaperone function.

Indexed as

Binding SitesEndopeptidase ClpEscherichia coli ProteinsGlutathione PeroxidaseHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesMutationPeptide Termination FactorsPrionsProtein Structure, TertiarySaccharomyces cerevisiae ProteinsClpB protein, E colidnaK protein, E coliEndopeptidase ClpEscherichia coli ProteinsGlutathione PeroxidaseHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSIS1 protein, S cerevisiaeSUP35 protein, S cerevisiaeURE2 protein, S cerevisiaeYDJ1 protein, S cerevisiae

Identifiers

PMID25329162
PMCPMC4199505
OpenAlexW1993161825

What OpenQuestion holds

Textmetadata
LicenceCC0
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.