Evidence map›Paper›PMID 32751253›Full record

ArticleCells2020

Nuclear Accumulation of LAP1:TRF2 Complex during DNA Damage Response Uncovers a Novel Role for LAP1.

Cátia D Pereira, Filipa Martins, Mariana Santos, Thorsten Müeller, Odete A B da Cruz E Silva, Sandra Rebelo

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. International journal of molecular sciences · 2023
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage Response.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Article
  15. Review
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 2 institutions in 2 countries.

Cátia D PereiraNeuroscience and Signaling Laboratory, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal.
Filipa MartinsNeuroscience and Signaling Laboratory, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0002-3277-1809
Mariana SantosNeuroscience and Signaling Laboratory, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0002-2343-2215
Thorsten MüellerCell Signaling in Neurodegeneration (CSIN), Medical Proteome-Center, Ruhr-University Bochum, 44801 Bochum, Germany.
Odete A B da Cruz E SilvaNeuroscience and Signaling Laboratory, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0003-3718-9874
Sandra RebeloNeuroscience and Signaling Laboratory, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0002-5862-5797
University of Aveiro · PTRuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lamina-associated polypeptide 1 (LAP1) is a nuclear envelope (NE) protein whose function remains poorly characterized. In a recent LAP1 protein interactome study, a putative regulatory role in the DNA damage response (DDR) has emerged and telomeric repeat-binding factor 2 (TRF2), a protein intimately associated with this signaling pathway, was among the list of LAP1 interactors. To gain insights into LAP1's physiological properties, the interaction with TRF2 in human cells exposed to DNA-damaging agents was investigated. The direct LAP1:TRF2 binding was validated in vitro by blot overlay and in vivo by co-immunoprecipitation after hydrogen peroxide and bleomycin treatments. The regulation of this protein interaction by LAP1 phosphorylation was demonstrated by co-immunoprecipitation and mass spectrometry following okadaic acid exposure. The involvement of LAP1 and TRF2 in the DDR was confirmed by their increased nuclear protein levels after bleomycin treatment, evaluated by immunoblotting, as well as by their co-localization with DDR factors at the NE and within the nucleoplasm, assessed by immunocytochemistry. Effectively, we showed that the LAP1:TRF2 complex is established during a cellular response against DNA damage. This work proposes a novel functional role for LAP1 in the DDR, revealing a potential biological mechanism that may be disrupted in LAP1-associated pathologies.

Indexed as

Ataxia Telangiectasia Mutated ProteinsBleomycinCell NucleusDNA DamageHeLa CellsHistonesHSC70 Heat-Shock ProteinsHumansHydrogen PeroxideMultiprotein ComplexesNuclear EnvelopePhosphorylationProtein BindingSignal TransductionTelomeric Repeat Binding Protein 2Ataxia Telangiectasia Mutated ProteinsATM protein, humanBleomycinH2AX protein, humanHistonesHSC70 Heat-Shock ProteinsHSPA8 protein, humanHydrogen PeroxideMultiprotein ComplexesTelomeric Repeat Binding Protein 2TERF2 protein, humanbleomycinDNA damageDNA repairhydrogen peroxideLAP1nuclear envelopenucleoplasmprotein phosphorylationTRF2γ-H2AX

Identifiers

PMID32751253
PMCPMC7465990
OpenAlexW3045543182

What OpenQuestion holds

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LicenceCC BY
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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.