Evidence map›Paper›PMID 39632680›Full record

ArticleEpigenomics2025

Emergent properties of the lysine methylome reveal regulatory roles via protein interactions and histone mimicry.

Gareth Pollin, Young-In Chi, Angela J Mathison, Michael T Zimmermann, Gwen Lomberk, Raul Urrutia

Abstract read
In one paragraph

Article in Epigenomics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Gareth PollinLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.ORCID 0000-0002-2787-6673
Young-In ChiLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.
Angela J MathisonLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.
Michael T ZimmermannLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.
Gwen LomberkLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.ORCID 0000-0001-5463-789X
Raul UrrutiaLinda T. and John A. Mellowes Center for Genomic Sciences and Precision Medicine (Mellowes Center), Medical College of Wisconsin, Milwaukee, WI, USA.ORCID 0000-0002-1640-6780

Funding

ZINC FINGER GENES AND PANCREATIC CELL GROWTHR01DK052913 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI LOMBERK, GWEN, URRUTIA, RAUL A. · 1998 to 2023
$7.0M
Targeting Epigenomic Regulators at the Replication Fork in PDACR01CA247898 · NCI · MEDICAL COLLEGE OF WISCONSIN · PI LOMBERK, GWEN · 2021 to 2025
$2.3M
Insights into EHMT1 Variants in the Neurodevelopmental Disorder Kleefstra Syndrome through Structural Dynamics and Functional AnalysisR21HD116120 · NICHD · MEDICAL COLLEGE OF WISCONSIN · PI CHI, YOUNG-IN, URRUTIA, RAUL A. · 2024 to 2024
$429k
NCI NIH HHS R01 CA247898NICHD NIH HHS R21 HD116120NIDDK NIH HHS R01 DK052913
6 · The paper itself

Abstract

aimsEpigenomics has significantly advanced through the incorporation of Systems Biology approaches. This study aims to investigate the human lysine methylome as a system, using a data-science approach to reveal its emergent properties, particularly focusing on histone mimicry and the broader implications of lysine methylation across the proteome.

methodsWe employed a data-science-driven OMICS approach, leveraging high-dimensional proteomic data to study the lysine methylome. The analysis focused on identifying sequence-based recognition motifs of lysine methyltransferases and evaluating the prevalence and distribution of lysine methylation across the human proteome.

resultsOur analysis revealed that lysine methylation impacts 15% of the known proteome, with a notable bias toward mono-methylation. We identified sequence-based recognition motifs of 13 lysine methyltransferases, highlighting candidates for histone mimicry. These findings suggest that the selective inhibition of individual lysine methyltransferases could have systemic effects rather than merely targeting histone methylation.

conclusionsThe lysine methylome has significant mechanistic value and should be considered in the design and testing of therapeutic strategies, particularly in precision oncology. The study underscores the importance of considering non-histone proteins involved in DNA damage and repair, cell signaling, metabolism, and cell cycle pathways when targeting lysine methyltransferases.

Indexed as

EpigenomeHistonesLysineHistone-Lysine N-MethyltransferaseHumansMethylationProtein Processing, Post-TranslationalProteomeProteomicsHistone-Lysine N-MethyltransferaseHistonesLysineProteomeBRD4epigeneticshistone mimicryLysine methylomemethylationmethyltransferasesmolecular dynamicspost-translational modification

Identifiers

PMID39632680
PMCPMC11703355

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Registered trials

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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.