Evidence map›Paper›PMID 21804533›Full record

ArticleThe EMBO journal2011

Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding.

Masayoshi Honda, Yusuke Okuno, Jungmin Yoo, Taekjip Ha, Maria Spies

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 15% 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

48 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.

  1. The Role of c-Abl in Alzheimer's Disease: Guilty or not Guilty?Cellular and molecular neurobiology · 2025
    Pooled it
  2. Targeting RAD52 overcomes PARP inhibitor resistance in preclinicalbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Detection assay of polymyxin resistance codingFrontiers in cellular and infection microbiology · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. A Facile Platform to EngineerACS central science · 2022
    Article
  12. Article
  13. Review
  14. Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021
    Review
  15. Article
  16. Review
  17. Inhibition of DNA Repair in Cancer Therapy: Toward a Multi-Target Approach.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. Cancers · 2019
    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

5 authors at 1 institution in 1 country.

Masayoshi HondaDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Yusuke Okuno
Jungmin Yoo
Taekjip Ha
Maria Spies
University of Illinois Urbana-Champaign · US

Funding

Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
NIGMS NIH HHS GM 065367NIGMS NIH HHS R01 GM065367
6 · The paper itself

Abstract

RAD52 protein has an important role in homology-directed DNA repair by mediating RAD51 nucleoprotein filament formation on single-stranded DNA (ssDNA) protected by replication protein-A (RPA) and annealing of RPA-coated ssDNA. In human, cellular response to DNA damage includes phosphorylation of RAD52 by c-ABL kinase at tyrosine 104. To address how this phosphorylation modulates RAD52 function, we used an amber suppressor technology to substitute tyrosine 104 with chemically stable phosphotyrosine analogue (p-Carboxymethyl-L-phenylalanine, pCMF). The RAD52(Y104pCMF) retained ssDNA-binding activity characteristic of unmodified RAD52 but showed lower affinity for double-stranded DNA (dsDNA) binding. Single-molecule analyses revealed that RAD52(Y104pCMF) specifically targets and wraps ssDNA. While RAD52(Y104pCMF) is confined to ssDNA region, unmodified RAD52 readily diffuses into dsDNA region. The Y104pCMF substitution also increased the ssDNA annealing rate and allowed overcoming the inhibitory effect of dsDNA. We propose that phosphorylation at Y104 enhances ssDNA annealing activity of RAD52 by attenuating dsDNA binding. Implications of phosphorylation-mediated activation of RAD52 annealing activity are discussed.

Indexed as

Protein Processing, Post-TranslationalAmino AcidsAmino Acid SequenceAmino Acid SubstitutionBinding, CompetitiveDNADNA Breaks, Double-StrandedDNA, Single-StrandedGenes, SuppressorHumansModels, MolecularMolecular Sequence DataPhenylalaninePhosphorylationPhosphotyrosineProtein Binding4-carboxymethylphenylalanineAmino AcidsDNADNA, Single-StrandedPhenylalaninePhosphotyrosineProto-Oncogene Proteins c-ablRad52 DNA Repair and Recombination ProteinRAD52 protein, humanRecombinant Fusion Proteins

Identifiers

PMID21804533
PMCPMC3160658
OpenAlexW1762536477

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.