Evidence map›Paper›PMID 27113759›Full record

ArticleEMBO reports2016

ATM/ATR-mediated phosphorylation of PALB2 promotes RAD51 function.

Johanna K Ahlskog, Brian D Larsen, Kavya Achanta, Claus S Sørensen

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2016. 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
4.4field-weighted citation impact, top 5% 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, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Targeting ATR in patients with cancer.Nature reviews. Clinical oncology · 2024
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. RAD51 wrestles with SUMO.Molecular & cellular oncology · 2022
    Article
  17. Article
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Johanna K AhlskogBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Brian D LarsenBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Kavya AchantaBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Claus S SørensenBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark claus.storgaard@bric.ku.dk.ORCID 0000-0001-6022-9710
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA damage activates the ATM and ATR kinases that coordinate checkpoint and DNA repair pathways. An essential step in homology-directed repair (HDR) of DNA breaks is the formation of RAD51 nucleofilaments mediated by PALB2-BRCA2; however, roles of ATM and ATR in this critical step of HDR are poorly understood. Here, we show that PALB2 is markedly phosphorylated in response to genotoxic stresses such as ionizing radiation and hydroxyurea. This response is mediated by the ATM and ATR kinases through three N-terminal S/Q-sites in PALB2, the consensus target sites for ATM and ATR Importantly, a phospho-deficient PALB2 mutant is unable to support proper RAD51 foci formation, a key PALB2 regulated repair event, whereas a phospho-mimicking PALB2 version supports RAD51 foci formation. Moreover, phospho-deficient PALB2 is less potent in HDR than wild-type PALB2. Further, this mutation reveals a separation in PALB2 function, as the PALB2-dependent checkpoint response is normal in cells expressing the phospho-deficient PALB2 mutant. Collectively, our findings highlight a critical importance of PALB2 phosphorylation as a novel regulatory step in genome maintenance after genotoxic stress.

Indexed as

ActinsAtaxia Telangiectasia Mutated ProteinsCell LineDNA DamageFanconi Anemia Complementation Group N ProteinGenomic InstabilityHumansHydroxyureaNuclear ProteinsPhosphorylationProtein BindingProtein Interaction Domains and MotifsRad51 RecombinaseRadiation, IonizingSerineTumor Suppressor ProteinsActinsAtaxia Telangiectasia Mutated ProteinsATR protein, humanFanconi Anemia Complementation Group N ProteinHydroxyureaNuclear ProteinsPALB2 protein, humanRad51 RecombinaseSerineTumor Suppressor ProteinsATMATRDNA damage responsePALB2 phosphorylationRAD51

Identifiers

PMID27113759
PMCPMC5341514
OpenAlexW2336734088

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.