Evidence map›Paper›PMID 19889838›Full record

ArticleMolecular biology of the cell2010

Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast.

Hugo Tapia, Kevin A Morano

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.

  1. Pooled it
  2. Identification of thePlants (Basel, Switzerland) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Genome-Wide Identification ofPlants (Basel, Switzerland) · 2021
    Article
  10. Cellular quiescence in budding yeast.Yeast (Chichester, England) · 2021
    Review
  11. Journal of fungi (Basel, Switzerland) · 2020
    Article
  12. Article
  13. Review
  14. The Nuclear and DNA-Associated Molecular Chaperone Network.Cold Spring Harbor perspectives in biology · 2019
    Review
  15. Article
  16. Article
  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

2 authors at 1 institution in 1 country.

Hugo TapiaDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, TX 77030, USA.
Kevin A Morano
The University of Texas Health Science Center at Houston · US

Funding

Hsp110 protein chaperone function in yeastR01GM074696 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MORANO, KEVIN ANTHONY · 2006 to 2015
$2.8M
NIGMS NIH HHS GM-074696NIGMS NIH HHS R01 GM074696
6 · The paper itself

Abstract

The 90-kDa heat-shock protein (Hsp90) operates in the context of a multichaperone complex to promote maturation of nuclear and cytoplasmic clients. We have discovered that Hsp90 and the cochaperone Sba1/p23 accumulate in the nucleus of quiescent Saccharomyces cerevisiae cells. Hsp90 nuclear accumulation was unaffected in sba1Delta cells, demonstrating that Hsp82 translocates independently of Sba1. Translocation of both chaperones was dependent on the alpha/beta importin SRP1/KAP95. Hsp90 nuclear retention was coincident with glucose exhaustion and seems to be a starvation-specific response, as heat shock or 10% ethanol stress failed to elicit translocation. We generated nuclear accumulation-defective HSP82 mutants to probe the nature of this targeting event and identified a mutant with a single amino acid substitution (I578F) sufficient to retain Hsp90 in the cytoplasm in quiescent cells. Diploid hsp82-I578F cells exhibited pronounced defects in spore wall construction and maturation, resulting in catastrophic sporulation. The mislocalization and sporulation phenotypes were shared by another previously identified HSP82 mutant allele. Pharmacological inhibition of Hsp90 with macbecin in sporulating diploid cells also blocked spore formation, underscoring the importance of this chaperone in this developmental program.

Indexed as

Allelesalpha Karyopherinsbeta KaryopherinsCell NucleusGlucoseHSP90 Heat-Shock ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpores, Fungalalpha Karyopherinsbeta KaryopherinsGlucoseHSP90 Heat-Shock ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19889838
PMCPMC2801720
OpenAlexW2104518674

What OpenQuestion holds

Textmetadata
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.