Evidence map›Paper›PMID 39698834›Full record

ArticleNucleic acids research2025

PRMT1-mediated methylation regulates MLL2 stability and gene expression.

Dongju An, Jihyun Kim, Byul Moon, Hyoungmin Kim, Hoa Nguyen, Sunghu Park, J Eugene Lee, Jung-Ae Kim, Jaehoon Kim

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

9 authors.

Dongju AnDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Jihyun KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Byul MoonAging Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, South Korea.
Hyoungmin KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Hoa NguyenDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Sunghu ParkDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
J Eugene LeeDivision of Biomedical Metrology, Korea Research Institute of Standards and Science, Daejeon 34113, South Korea.
Jung-Ae KimAging Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, South Korea.ORCID 0000-0001-5485-4843
Jaehoon KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.ORCID 0000-0003-4035-0438

Funding

National Research Foundation of Korea NRF-2022R1A2C3012803
6 · The paper itself

Abstract

The interplay between multiple transcription factors precisely regulates eukaryotic transcription. Here, we report that the protein methyltransferases, MLL2/KMT2B and PRMT1, interact directly and act collectively to regulate gene expression. PRMT1 binds to the N-terminal region of MLL2, considered an intrinsically disordered region, and methylates multiple arginine residues within its RGG/RG motifs. Notably, overexpression of PRMT1 decreased poly-ubiquitylation of MLL2, whereas mutations on methylation sites in MLL2 increased MLL2 poly-ubiquitylation, suggesting that PRMT1-mediated methylation stabilizes MLL2. MLL2 and PRMT1 cooperatively stimulated the expression of a chromosomal reporter gene in a PRMT1-mediated, MLL2-methylation-dependent manner. RNA-seq analysis found that MLL2 and PRMT1 jointly regulate the expression of genes involved in cell membrane and extracellular matrix functions, and depletion of either resulted in impaired cell migration and invasion. Our study provides evidence that PRMT1-mediated MLL2 methylation regulates MLL2 protein stability and the expression of their target genes.

Indexed as

DNA-Binding ProteinsGene Expression RegulationNeoplasm ProteinsProtein-Arginine N-MethyltransferasesRepressor ProteinsCell MovementHEK293 CellsHumansMethylationProtein BindingProtein StabilityUbiquitinationDNA-Binding ProteinsKMT2D protein, humanNeoplasm ProteinsPRMT1 protein, humanProtein-Arginine N-MethyltransferasesRepressor Proteins

Identifiers

PMID39698834
PMCPMC11879031

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.