Evidence map›Paper›PMID 25631054›Full record

ArticleThe Journal of biological chemistry2015

Differential phosphorylation of a regulatory subunit of protein kinase CK2 by target of rapamycin complex 1 signaling and the Cdc-like kinase Kns1.

Manuel E Sanchez-Casalongue, Jaehoon Lee, Aviva Diamond, Scott Shuldiner, Robyn D Moir, Ian M Willis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Pleiotropic roles of LAMMER kinase, Lkh1 in stress responses and virulence ofFrontiers in cellular and infection microbiology · 2024
    Article
  5. Review
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  7. Article
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  9. Article
  10. Review
  11. Article
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  13. Review
  14. Review
  15. Review
  16. Azole resistance in aThe Journal of biological chemistry · 2018
    Article
  17. Article
  18. Article
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  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

6 authors at 1 institution in 1 country.

Manuel E Sanchez-CasalongueFrom the Departments of Biochemistry and.
Jaehoon LeeFrom the Departments of Biochemistry and.
Aviva DiamondFrom the Departments of Biochemistry and.
Scott ShuldinerFrom the Departments of Biochemistry and.
Robyn D MoirFrom the Departments of Biochemistry and.
Ian M WillisFrom the Departments of Biochemistry and Systems and Computational Biology, Albert Einstein College of Medicine, Bronx, New York 10461 ian.willis@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
Special Animal CoreP30DK041296 · NIDDK · YESHIVA UNIVERSITY · PI WOLKOFF, ALLAN W · 1989 to 2018
$22.9M
Transcriptional Repression by Maf1 in YeastR01GM085177 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI WILLIS, IAN M · 2009 to 2012
$2.1M
NIDDK NIH HHS P30 DK041296NIGMS NIH HHS R01 GM085177NIGMS NIH HHS T32-GM007288
6 · The paper itself

Abstract

Transcriptional regulation of ribosome and tRNA synthesis plays a central role in determining protein synthetic capacity and is tightly controlled in response to nutrient availability and cellular stress. In Saccharomyces cerevisiae, the regulation of ribosome and tRNA synthesis was recently shown to involve the Cdc-like kinase Kns1 and the GSK-3 kinase Mck1. In this study, we explored additional roles for these conserved kinases in processes connected to the target of rapamycin complex 1 (TORC1). We conducted a synthetic chemical-genetic screen in a kns1Δ mck1Δ strain and identified many novel rapamycin-hypersensitive genes. Gene ontology analysis showed enrichment for TORC1-regulated processes (vesicle-mediated transport, autophagy, and regulation of cell size) and identified new connections to protein complexes including the protein kinase CK2. CK2 is considered to be a constitutively active kinase and in budding yeast, the holoenzyme comprises two regulatory subunits, Ckb1 and Ckb2, and two catalytic subunits, Cka1 and Cka2. We show that Ckb1 is differentially phosphorylated in vivo and that Kns1 mediates this phosphorylation when nutrients are limiting and under all tested stress conditions. We determined that the phosphorylation of Ckb1 does not detectably affect the stability of the CK2 holoenzyme but correlates with the reduced occupancy of Ckb1 on tRNA genes after rapamycin treatment. Thus, the differential occupancy of tRNA genes by CK2 is likely to modulate its activation of RNA polymerase III transcription. Our data suggest that TORC1, via its effector kinase Kns1, may regulate the association of CK2 with some of its substrates by phosphorylating Ckb1.

Indexed as

Signal TransductionAntifungal AgentsCasein Kinase IIGene DeletionGene Expression Regulation, FungalMutationPhosphorylationProtein Serine-Threonine KinasesProtein SubunitsRNA Polymerase IIISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSirolimusStress, PhysiologicalTranscriptional ActivationTranscription FactorsAntifungal AgentsCasein Kinase IIKNS1 protein, S cerevisiaeProtein Serine-Threonine KinasesProtein SubunitsRNA Polymerase IIISaccharomyces cerevisiae ProteinsSirolimusTORC1 protein complex, S cerevisiaeTranscription FactorsCellular RegulationGlycogen Synthase Kinase 3 (GSK-3)Protein KinaseRNA Polymerase IIITarget of Rapamycin (TOR)Transcription

Identifiers

PMID25631054
PMCPMC4358141
OpenAlexW2025678066

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.