Evidence map›Paper›PMID 24958100›Full record

ArticleMolecular and cellular biology2014

Yeast Dun1 kinase regulates ribonucleotide reductase inhibitor Sml1 in response to iron deficiency.

Nerea Sanvisens, Antonia M Romero, Xiuxiang An, Caiguo Zhang, Rosa de Llanos, María Teresa Martínez-Pastor, M Carmen Bañó, Mingxia Huang, Sergi Puig

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

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  7. Adaptation ofInternational journal of molecular sciences · 2022
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  11. DNA damage checkpoint execution and the rules of its disengagement.Frontiers in cell and developmental biology · 2022
    Review
  12. Sterol Composition Modulates the Response ofJournal of fungi (Basel, Switzerland) · 2021
    Article
  13. Article
  14. Iron Regulatory Mechanisms inFrontiers in microbiology · 2020
    Review
  15. Article
  16. Article
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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

9 authors at 4 institutions in 2 countries.

Nerea SanvisensDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), Paterna, Valencia, Spain.
Antonia M RomeroDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), Paterna, Valencia, Spain.
Xiuxiang AnDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Denver, Colorado, USA.
Caiguo ZhangDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Denver, Colorado, USA.
Rosa de LlanosDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), Paterna, Valencia, Spain.
María Teresa Martínez-PastorDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Valencia, Spain.
M Carmen BañóDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Valencia, Spain.
Mingxia HuangDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Denver, Colorado, USA mingxia.huang@ucdenver.edu spuig@iata.csic.es.
Sergi PuigDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), Paterna, Valencia, Spain mingxia.huang@ucdenver.edu spuig@iata.csic.es.
Instituto de Agroquímica y Tecnología de Alimentos · ESUniversity of Colorado Denver · USUniversitat de València · ESConsejo Superior de Investigaciones Científicas · ES

Funding

In Vivo Regulation and Inhibition of Ribonucleotide ReductaseR01CA125574 · NCI · UNIVERSITY OF COLORADO DENVER · PI HUANG, MINGXIA · 2008 to 2012
$1.6M
NCI NIH HHS CA125574NCI NIH HHS R01 CA125574
6 · The paper itself

Abstract

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar proteolytic pathway. Depletion of core components of the mitochondrial iron-sulfur cluster assembly leads to a Dun1-dependent diminution of Sml1 protein levels. The physiological relevance of Sml1 downregulation by Dun1 under low-Fe conditions is highlighted by the synthetic growth defect observed between dun1Δ and fet3Δ fet4Δ mutants, which is rescued by SML1 deletion. Consistent with an increase in RNR function, Rnr1 protein levels are upregulated upon Fe deficiency. Finally, dun1Δ mutants display defects in deoxyribonucleoside triphosphate (dNTP) biosynthesis under low-Fe conditions. Taken together, these results reveal that the Dun1 checkpoint kinase promotes RNR function in response to Fe starvation by stimulating Sml1 protein degradation.

Indexed as

Aspartic Acid EndopeptidasesBinding SitesCell Cycle ProteinsCheckpoint Kinase 2DeoxyribonucleotidesDNA-Binding ProteinsGene DeletionGenes, FungalIntracellular Signaling Peptides and ProteinsIronIron-Sulfur ProteinsPhosphorylationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProteolysisRibonucleotide ReductasesAFT1 protein, S cerevisiaeAspartic Acid EndopeptidasesATP dependent 26S proteaseCell Cycle ProteinsCheckpoint Kinase 2CTH1 protein, S cerevisiaeDeoxyribonucleotidesDNA-Binding ProteinsDUN1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsIronIron-Sulfur ProteinsMEC1 protein, S cerevisiaePEP4 protein, S cerevisiaeProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeRibonucleotide ReductasesRnr1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSML1 protein, S cerevisiaeTIS11 protein, S cerevisiaeTranscription FactorsTristetraprolin

Identifiers

PMID24958100
PMCPMC4135553
OpenAlexW2105455714

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.