Evidence map›Paper›PMID 31024071›Full record

ArticleScientific reports2019

The nuclear interactome of DYRK1A reveals a functional role in DNA damage repair.

Steven E Guard, Zachary C Poss, Christopher C Ebmeier, Maria Pagratis, Helen Simpson, Dylan J Taatjes, William M Old

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
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  7. Calcineurin inhibition may prevent Alzheimer disease in people with Down syndrome.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  8. Article
  9. DYRK1A roles in human neural progenitors.Frontiers in neuroscience · 2025
    Article
  10. Article
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  14. Article
  15. Review
  16. 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

7 authors at 1 institution in 1 country.

Steven E GuardDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.
Zachary C PossDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.
Christopher C EbmeierDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.
Maria PagratisDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.
Helen SimpsonDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.
Dylan J TaatjesDepartment of Biochemistry, University of Colorado, Boulder, CO, USA.
William M OldDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA. William.Old@colorado.edu.ORCID http://orcid.org/0000-0002-9499-8478
University of Colorado Boulder · US

Funding

TFIIH and Transcription RegulationR01GM110064 · NIGMS · UNIVERSITY OF COLORADO · PI RANISH, JEFFREY A, TAATJES, DYLAN J · 2016 to 2019
$2.2M
NIGMS NIH HHS R01 GM110064
6 · The paper itself

Abstract

The chromosome 21 encoded protein kinase DYRK1A is essential for normal human development. Mutations in DYRK1A underlie a spectrum of human developmental disorders, and increased dosage in trisomy 21 is implicated in Down syndrome related pathologies. DYRK1A regulates a diverse array of cellular processes through physical interactions with substrates and binding partners in various subcellular compartments. Despite recent large-scale protein-protein interaction profiling efforts, DYRK1A interactions specific to different subcellular compartments remain largely unknown, impeding progress toward understanding emerging roles for this kinase. Here, we used immunoaffinity purification and quantitative mass spectrometry to identify nuclear interaction partners of endogenous DYRK1A. This interactome was enriched in DNA damage repair factors, transcriptional elongation factors and E3 ubiquitin ligases. We validated an interaction with RNF169, a factor that promotes homology directed repair upon DNA damage, and found that DYRK1A expression and kinase activity are required for maintenance of 53BP1 expression and subsequent recruitment to DNA damage loci. Further, DYRK1A knock out conferred resistance to ionizing radiation in colony formation assays, suggesting that DYRK1A expression decreases cell survival efficiency in response to DNA damage and points to a tumor suppressive role for this kinase.

Indexed as

DNA DamageDNA RepairProtein Interaction MapsCell NucleusCell SurvivalDyrk KinasesHEK293 CellsHeLa CellsHumansProtein BindingProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRadiation, IonizingTumor Suppressor p53-Binding Protein 1Ubiquitin-Protein LigasesDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRNF169 protein, humanTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1Ubiquitin-Protein Ligases

Identifiers

PMID31024071
PMCPMC6483993
OpenAlexW2950456028

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.