Evidence map›Paper›PMID 15643056›Full record

ArticleEukaryotic cell2005

Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.

Miguel Arévalo-Rodríguez, Joseph Heitman

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Structural and functional analysis of the SET3 histone deacetylase complex.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  4. Review
  5. Review
  6. Review
  7. Functional Analysis of Peptidyl-prolylInternational journal of molecular sciences · 2019
    Article
  8. Article
  9. Review
  10. Microbial cyclophilins: specialized functions in virulence and beyond.World journal of microbiology & biotechnology · 2017
    Review
  11. Article
  12. Article
  13. Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015
    Review
  14. Article
  15. Article
  16. Article
  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

2 authors at 1 institution in 1 country.

Miguel Arévalo-RodríguezDepartment of Molecular Genetics and Microbiology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA.
Joseph Heitman
Duke Medical Center · US

Funding

Novel Antifungal Therapeutic ApproachesR01AI050438 · NIAID · DUKE UNIVERSITY · PI HEITMAN, JOSEPH · 2001 to 2012
$3.3M
NIAID NIH HHS 1R01 AI-50438NIAID NIH HHS R01 AI050438
6 · The paper itself

Abstract

Cyclophilin A is conserved from yeast to humans and mediates the ability of cyclosporine to perturb signal transduction cascades via inhibition of calcineurin. Cyclophilin A also catalyzes cis-trans peptidyl-prolyl isomerization during protein folding or conformational changes; however, cyclophilin A is not essential in yeast or human cells, and the true biological functions of this highly conserved enzyme have remained enigmatic. In Saccharomyces cerevisiae, cyclophilin A becomes essential in cells compromised for the nuclear prolyl-isomerase Ess1, and cyclophilin A physically interacts with two nuclear histone deacetylase complexes, Sin3-Rpd3 and Set3C, which both control meiosis. Here we show that cyclophilin A is localized to the nucleus in yeast cells and governs the meiotic gene program to promote efficient sporulation. The prolyl-isomerase activity of cyclophilin A is required for this meiotic function. We document that cyclophilin A physically associates with the Set3C histone deacetylase and analyze in detail the structure of this protein-protein complex. Genetic studies support a model in which cyclophilin A controls meiosis via Set3C and an additional target. Our findings reveal a novel nuclear role for cyclophilin A in governing the transcriptional program required for the vegetative to meiotic developmental switch in budding yeast.

Indexed as

Gene Expression Regulation, DevelopmentalMeiosisBlotting, NorthernBlotting, WesternCell NucleusCyclophilin ACytoplasmElectrophoresis, Polyacrylamide GelGreen Fluorescent ProteinsHistone DeacetylasesImmunoprecipitationModels, BiologicalNIMA-Interacting Peptidylprolyl IsomeraseOligonucleotidesPeptidylprolyl IsomerasePlasmidsCyclophilin AESS1 protein, S cerevisiaeGreen Fluorescent ProteinsHistone DeacetylasesNIMA-Interacting Peptidylprolyl IsomeraseOligonucleotidesPeptidylprolyl IsomerasePIN1 protein, humanRecombinant Fusion ProteinsRepressor ProteinsRPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIN3 protein, S cerevisiaeTranscription Factors

Identifiers

PMID15643056
PMCPMC544151
OpenAlexW2124061766

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.