Evidence map›Paper›PMID 22851130›Full record

ArticleMolecular bioSystems2012

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones.

Anne T Gillies, Rebecca Taylor, Jason E Gestwicki

Open access · greenAbstract read
In one paragraph

Article in Molecular bioSystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Article
  3. Transcriptomic Analysis of Copper Resistance inAntibiotics (Basel, Switzerland) · 2025
    Article
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  6. ACS omega · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Transcriptional responses ofNPJ biofilms and microbiomes · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Anne T GilliesDepartments of Pathology and Biological Chemistry and the Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA.
Rebecca Taylor
Jason E Gestwicki
Washtenaw Community College · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
NIGMS NIH HHS GM008353NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304NINDS NIH HHS NS059690NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

J proteins are a diverse family of co-chaperones that cooperate with heat shock protein 70 (Hsp70) to coordinate protein quality control, especially in response to cellular stress. Current models suggest that individual J proteins might play roles in recruiting Hsp70s to specific functions, such as maintaining cell wall integrity or promoting ribosome biogenesis. However, relatively few stresses have been used to test this model and, as a result, only a few specific activities have been identified. To expand our understanding of the J protein network, we used a synthetic lethal approach in which 11 Saccharomyces cerevisiae deletion strains were treated with 12 well-characterized chemical inhibitors. The results defined new roles for specific J proteins in major signaling pathways. For example, an important role for Swa2 in cell wall integrity was identified and activities of the under-explored Jjj1, Apj1, Jjj3 and Caj1 proteins were suggested. More generally, these findings support a model in which some J proteins, such as Ydj1 and Zuo1, play "generalist" roles, while others, such as Apj1 and Jjj2, are "specialists", having roles in relatively few pathways. Together, these results provide new insight into the network of J proteins.

Indexed as

Calmodulin-Binding ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPhosphoproteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionVesicular Transport ProteinsAPJ1 protein, S cerevisiaeCAJ1 protein, S cerevisiaeCalmodulin-Binding ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsJjj1 protein, S cerevisiaeMolecular ChaperonesPhosphoproteinsSaccharomyces cerevisiae ProteinsSWA2 protein, S cerevisiaeVesicular Transport ProteinsYDJ1 protein, S cerevisiae

Identifiers

PMID22851130
PMCPMC3463740
OpenAlexW2138238729

What OpenQuestion holds

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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.