Evidence map›Paper›PMID 32235358›Full record

ArticleInternational journal of molecular sciences2020

The Subcellular Localization and Oligomerization Preferences of NME1/NME2 upon Radiation-Induced DNA Damage.

Martina Radić, Marko Šoštar, Igor Weber, Helena Ćetković, Neda Slade, Maja Herak Bosnar

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. NucleariScience · 2024
    Article
  3. Article
  4. Article
  5. p53 Family in Resistance to Targeted Therapy of Melanoma.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  11. 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.

Martina RadićDivision of Molecular Medicine, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Marko ŠoštarDivision of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Igor WeberDivision of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.ORCID 0000-0003-4296-3166
Helena ĆetkovićDivision of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Neda SladeDivision of Molecular Medicine, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Maja Herak BosnarDivision of Molecular Medicine, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Ruđer Bošković Institute · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoside diphosphate kinases (NDPK/NME/Nm23) are enzymes composed of subunits NME1/NDPK A and NME2/NDPK B, responsible for the maintenance of the cellular (d)NTP pool and involved in other cellular processes, such as metastasis suppression and DNA damage repair. Although eukaryotic NDPKs are active only as hexamers, it is unclear whether other NME functions require the hexameric form, and how the isoenzyme composition varies in different cellular compartments. To examine the effect of DNA damage on intracellular localization of NME1 and NME2 and the composition of NME oligomers in the nucleus and the cytoplasm, we used live-cell imaging and the FRET/FLIM technique. We showed that exogenous NME1 and NME2 proteins co-localize in the cytoplasm of non-irradiated cells, and move simultaneously to the nucleus after gamma irradiation. The FRET/FLIM experiments imply that, after DNA damage, there is a slight shift in the homomer/heteromer balance between the nucleus and the cytoplasm. Collectively, our results indicate that, after irradiation, NME1 and NME2 engage in mutual functions in the nucleus, possibly performing specific functions in their homomeric states. Finally, we demonstrated that fluorophores fused to the N-termini of NME polypeptides produce the largest FRET effect and thus recommend this orientation for use in similar studies.

Indexed as

Radiation, IonizingAnimalsBiomarkersCell LineCell NucleusDNA DamageFluorescent Antibody TechniqueGamma RaysHumansNM23 Nucleoside Diphosphate KinasesProtein BindingProtein MultimerizationProtein TransportBiomarkersNM23 Nucleoside Diphosphate KinasesNME1 protein, humanNME2 protein, humanFLIMFRETlive-cell imagingNDPKNm23NMEnucleoside diphosphate kinase

Identifiers

PMID32235358
PMCPMC7177722
OpenAlexW3013594993

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Registered trials

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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.