Evidence map›Paper›PMID 23716636›Full record

ArticleNucleic acids research2013

Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair.

Ryotaro Nishi, Wataru Sakai, Daisuke Tone, Fumio Hanaoka, Kaoru Sugasawa

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. DNA Repair Mechanisms.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  2. Article
  3. Article
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  5. Review
  6. Article
  7. Article
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  9. Review
  10. Study on the interaction ofRSC advances · 2021
    Article
  11. Review
  12. Sufu negatively regulates both initiations of centrosome duplication and DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. XPA: DNA Repair Protein of Significant Clinical Importance.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Article
  19. Mechanism and regulation of DNA damage recognition in nucleotide excision repair.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2019
    Review
  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

5 authors at 2 institutions in 1 country.

Ryotaro NishiBiosignal Research Center, Organization of Advanced Science and Technology, Kobe University, Kobe, Hyogo 657-8501, Japan.
Wataru Sakai
Daisuke Tone
Fumio Hanaoka
Kaoru Sugasawa
Gakushuin University · JPKobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centrin-2 is an evolutionarily conserved, calmodulin-related protein, which is involved in multiple cellular functions including centrosome regulation and nucleotide excision repair (NER) of DNA. Particularly to exert the latter function, complex formation with the XPC protein, the pivotal NER damage recognition factor, is crucial. Here, we show that the C-terminal half of centrin-2, containing two calcium-binding EF-hand motifs, is necessary and sufficient for both its localization to the centrosome and interaction with XPC. In XPC-deficient cells, nuclear localization of overexpressed centrin-2 largely depends on co-overexpression of XPC, and mutational analyses of the C-terminal domain suggest that XPC and the major binding partner in the centrosome share a common binding surface on the centrin-2 molecule. On the other hand, the N-terminal domain of centrin-2 also contains two EF-hand motifs but shows only low-binding affinity for calcium ions. Although the N-terminal domain is dispensable for enhancement of the DNA damage recognition activity of XPC, it contributes to augmenting rather weak physical interaction between XPC and XPA, another key factor involved in NER. These results suggest that centrin-2 may have evolved to bridge two protein factors, one with high affinity and the other with low affinity, thereby allowing delicate regulation of various biological processes.

Indexed as

DNA RepairCalcium-Binding ProteinsCell Cycle ProteinsCell LineCell NucleusDNA-Binding ProteinsDNA DamageHumansProtein Structure, TertiaryStructure-Activity RelationshipUltraviolet RaysXeroderma Pigmentosum Group A ProteinCalcium-Binding ProteinsCell Cycle ProteinsCETN2 protein, humanDNA-Binding ProteinsXeroderma Pigmentosum Group A ProteinXPC protein, human

Identifiers

PMID23716636
PMCPMC3737541
OpenAlexW2034593148

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.