Evidence map›Paper›PMID 23707759›Full record

ArticleMolecular cell2013

A method for systematic mapping of protein lysine methylation identifies functions for HP1β in DNA damage response.

Huadong Liu, Marek Galka, Eiichiro Mori, Xuguang Liu, Yu-Fen Lin, Ran Wei, Paula Pittock, Courtney Voss, Gurpreet Dhami, Xing Li and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.1field-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

56 citing papers in PubMed, 104 citations in OpenAlex.

  1. Mapping Cellular Protein Lysine Methylation Using Targeted-Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. The Role of Protein Methyltransferases in Immunity.Molecules (Basel, Switzerland) · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
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  14. Review
  15. Article
  16. eLife · 2020
    Article
  17. Review
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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

14 authors at 3 institutions in 2 countries.

Huadong LiuDepartment of Biochemistry and the Siebens-Drake Medical Research Institute, Schulich School of Medicine and Dentistry, University of Western Ontario, London, ON N6A 5C1, Canada.
Marek Galka
Eiichiro Mori
Xuguang Liu
Yu-Fen Lin
Ran Wei
Paula Pittock
Courtney Voss
Gurpreet Dhami
Xing Li
Masaaki Miyaji
Gilles Lajoie
Benjamin Chen
Shawn Shun-Cheng Li
Western University · CAThe University of Texas Southwestern Medical Center · USAdvanced Micro Devices (United States) · US

Funding

DNA-PKcs Phosphorylation on Hematopoietic Stem Cells Genome MaintenanceR01CA166677 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, BENJAMIN PING-CHI · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA166677
6 · The paper itself

Abstract

Lysine methylation occurs on both histone and nonhistone proteins. However, our knowledge on the prevalence and function of nonhistone protein methylation is poor. We describe an approach that combines peptide array, bioinformatics, and mass spectrometry to systematically identify lysine methylation sites and map methyllysine-driven protein-protein interactions. Using this approach, we identified a high-confidence and high-resolution interactome of the heterochromatin protein 1β (HP1β) and uncovered, simultaneously, numerous methyllysine sites on nonhistone proteins. We found that HP1β binds to DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and regulates its localization to double-strand breaks (DSBs) during DNA damage response (DDR). Mutation of the methylation sites in DNA-PKcs or depletion of HP1β in cells caused defects in DDR. Furthermore, we showed that the methylation of DNA-PKcs and many other proteins in the HP1β interactome undergoes large changes in response to DNA damage, indicating that Lys methylation is a highly dynamic posttranslational modification.

Indexed as

DNA DamageCatalytic DomainChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDNA-Activated Protein KinaseDNA Breaks, Double-StrandedHigh-Throughput Screening AssaysHumansLysineMethylationMutationProtein Processing, Post-TranslationalProteinsReproducibility of ResultsCBX1 protein, humanChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDNA-Activated Protein KinaseLysineProteins

Identifiers

PMID23707759
PMCPMC4032624
OpenAlexW2067080454

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.