Evidence map›Paper›PMID 16148046›Full record

ArticleMolecular biology of the cell2005

Role of the C terminus of Mec1 checkpoint kinase in its localization to sites of DNA damage.

Daisuke Nakada, Yukinori Hirano, Yuya Tanaka, Katsunori Sugimoto

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Mec1-mediated Atg9 phosphorylation regulates the PAS recruitment of Atg9 vesicles upon energy stress.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Mec1Cell reports · 2019
    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

4 authors at 1 institution in 1 country.

Daisuke NakadaDepartment of Cell Biology and Molecular Medicine, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, NJ 07103, USA.
Yukinori Hirano
Yuya Tanaka
Katsunori Sugimoto
Rutgers, The State University of New Jersey · US

Funding

Signaling network of Mec1 in DNA damage responseR01GM073876 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI SUGIMOTO, KATSUNORI · 2005 to 2013
$2.7M
NIGMS NIH HHS R01 GM-073876NIGMS NIH HHS R01 GM073876
6 · The paper itself

Abstract

The large protein kinases, ataxia-telangiectasia mutated (ATM) and ATM-Rad3-related (ATR), coordinate the cellular response to DNA damage. In budding yeast, ATR homologue Mec1 plays a central role in DNA damage signaling. Mec1 interacts physically with Ddc2 and functions in the form of the Mec1-Ddc2 complex. To identify proteins interacting with the Mec1-Ddc2 complex, we performed a modified two-hybrid screen and isolated RFA1 and RFA2, genes that encode subunits of replication protein A (RPA). Using the two-hybrid system, we found that the extreme C-terminal region of Mec1 is critical for RPA binding. The C-terminal substitution mutation does not affect the Mec1-Ddc2 complex formation, but it does impair the interaction of Mec1 and Ddc2 with RPA as well as their association with DNA lesions. The C-terminal mutation also decreases Mec1 kinase activity. However, the Mec1 kinase-defect by itself does not perturb Mec1 association with sites of DNA damage. We also found that Mec1 and Ddc2 associate with sites of DNA damage in an interdependent manner. Our findings support the model in which Mec1 and Ddc2 localize to sites of DNA damage by interacting with RPA in the form of the Mec1-Ddc2 complex.

Indexed as

DNA DamageAdaptor Proteins, Signal TransducingAnimalsCell Cycle ProteinsDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsMutationPhosphoproteinsProtein Serine-Threonine KinasesReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsTwo-Hybrid System TechniquesAdaptor Proteins, Signal TransducingCell Cycle ProteinsDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsLCD1 protein, S cerevisiaeMEC1 protein, S cerevisiaePhosphoproteinsProtein Serine-Threonine KinasesReplication Protein ARFA1 protein, S cerevisiaeRFA2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID16148046
PMCPMC1266421
OpenAlexW2145902670

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.