Evidence map›Paper›PMID 18851834›Full record

ArticleMolecular cell2008

Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.

Yang David Lee, Jun Wang, Joanne Stubbe, Stephen J Elledge

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

73 citing papers in PubMed, 111 citations in OpenAlex.

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  11. The Molecular Mechanism of Perillaldehyde Inducing Cell Death inInternational journal of molecular sciences · 2020
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13 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Yang David LeeHarvard Medical School, Department of Genetics, Brigham and Women's Hospital, Center for Genetics and Genomics, Howard Hughes Medical Institute, Boston, MA 02115, USA.
Jun Wang
Joanne Stubbe
Stephen J Elledge
Brigham and Women's Hospital · USMassachusetts Institute of Technology · US

Funding

Genetics of Cell Cycle &DNA Damage Regulation in YeastR37GM044664 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI ELLEDGE, STEPHEN J · 2003 to 2012
$3.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R37 GM044664
6 · The paper itself

Abstract

The control of dNTP concentrations is critical to the fidelity of DNA synthesis and repair. One level of regulation is through subcellular localization of ribonucleotide reductase. In Saccharomyces cerevisiae, the small subunit Rnr2-Rnr4 is nuclear, whereas the large subunit Rnr1 is cytoplasmic. In response to S phase or DNA damage, Rnr2-Rnr4 enters the cytoplasm to bind Rnr1, forming an active complex. We previously reported that Wtm1 anchors Rnr2-Rnr4 in the nucleus. Here, we identify DIF1, which regulates localization of Rnr2-Rnr4. Dif1 binds directly to the Rnr2-Rnr4 complex through a conserved Hug domain to drive nuclear import. Dif1 is both cell-cycle and DNA-damage regulated, the latter of which occurs via the Mec1-Dun1 pathway. In response to DNA damage, Dun1 directly phosphorylates Dif1, which both inactivates and degrades Dif1 and allows Rnr2-Rnr4 to become cytoplasmic. We propose that Rnr2-Rnr4 nuclear localization is achieved by a dynamic combination of Wtm1-mediated nuclear retention to limit export and regulated nuclear import through Dif1.

Indexed as

DNA DamageActive Transport, Cell NucleusAmino Acid SequenceCell CycleConserved SequenceGenes, FungalIntracellular Signaling Peptides and ProteinsModels, BiologicalModels, MolecularMolecular Sequence DataMultiprotein ComplexesMutationPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMultiprotein ComplexesProtein Serine-Threonine KinasesRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesRnr4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsWnt1 Protein

Identifiers

PMID18851834
PMCPMC3245869
OpenAlexW2040120405

What OpenQuestion holds

Textmetadata
LicenceTDM
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.