Evidence map›Paper›PMID 22337769›Full record

ArticleMolecular biology of the cell2012

The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells.

I-Chun Liu, Sheng-Wen Chiu, Hsin-Yi Lee, Jun-Yi Leu

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
–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

36 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Quiescence inAnnual review of genetics · 2022
    Review
  11. Contributions of a Histone Deacetylase (SirT2/Hst2) toJournal of fungi (Basel, Switzerland) · 2022
    Article
  12. Moonlighting at the Poles: Non-Canonical Functions of Centrosomes.Frontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Review
  15. Review
  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

4 authors.

I-Chun LiuInstitute of Molecular Biology, Academia Sinica, Taipei 114, Taiwan.
Sheng-Wen Chiu
Hsin-Yi Lee
Jun-Yi Leu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of many physiological adjustments in quiescent cells is spatial regulation of specific proteins and RNA important for the entry to or exit from the stationary phase. By examining the localization of epigenetic-related proteins in Saccharomyces cerevisiae, we observed the formation of a reversible cytosolic "stationary-phase granule" (SPG) by Hos2, a nuclear histone deacetylase. In the stationary phase, hos2 mutants display reduced viability. Additionally, they exhibit a significant delay when recovering from stationary phase. Hos2 SPGs also contained Hst2, a Sir2 homologue, and several stress-related proteins, including Set3, Yca1, Hsp26, Hsp42, and some known components of stress granules. However, Hos2 SPG formation does not depend on the formation of stress granules or processing bodies. The absence or presence of glucose is sufficient to trigger assembly or disassembly of Hos2 SPGs. Among the identified components of Hos2 SPGs, Hsp42 is the first and last member observed in the Hos2 SPG assembly and disassembly processes. Hsp42 is also vital for the relocalization of the other components to Hos2 SPGs, suggesting that Hsp42 plays a central role in spatial regulation of proteins in quiescent cells.

Indexed as

Actin CytoskeletonCytoplasmic GranulesEpigenesis, GeneticGenes, FungalGlucoseHeat-Shock ProteinsHeat-Shock ResponseHistone DeacetylasesMutationProtein MultimerizationRecombinant Fusion ProteinsResting Phase, Cell CycleSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGlucoseHeat-Shock ProteinsHistone DeacetylasesHOS2 protein, S cerevisiaeHSP26 protein, S cerevisiaeHSP42 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSet3 protein, S cerevisiae

Identifiers

PMID22337769
PMCPMC3315813

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.