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Related Experiment Video

Updated: Jun 4, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

PRMT1-mediated methylation regulates MLL2 stability and gene expression.

Dongju An¹, Jihyun Kim¹, Byul Moon²

¹Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.

Nucleic Acids Research

|December 19, 2024

Summary

Protein methyltransferases MLL2 (KMT2B) and PRMT1 interact to regulate gene expression. PRMT1 methylation stabilizes MLL2, impacting cell functions like migration and invasion.

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Area of Science:

Molecular Biology
Epigenetics
Gene Regulation

Background:

Eukaryotic transcription is precisely regulated by the interplay of multiple transcription factors.
Protein methyltransferases play crucial roles in modulating protein function and stability.

Purpose of the Study:

To investigate the interaction and collective function of MLL2 (KMT2B) and PRMT1 in gene expression regulation.
To elucidate the mechanism by which PRMT1 affects MLL2 stability and activity.

Main Methods:

Co-immunoprecipitation to confirm protein-protein interaction.
Site-directed mutagenesis to identify methylation sites on MLL2.
Western blotting to assess protein ubiquitylation and stability.
Chromosomal reporter gene assays to measure transcriptional activity.
RNA-sequencing (RNA-seq) to analyze gene expression changes.
Gene depletion studies (e.g., siRNA or shRNA) to assess functional consequences.

Main Results:

MLL2 (KMT2B) and PRMT1 directly interact, with PRMT1 binding to the intrinsically disordered N-terminal region of MLL2.
PRMT1 methylates arginine residues in MLL2's RGG/RG motifs, decreasing MLL2 poly-ubiquitylation and enhancing its stability.
PRMT1-mediated MLL2 methylation cooperatively stimulates gene expression in a methylation-dependent manner.
Jointly regulated genes are involved in cell membrane and extracellular matrix functions.
Depletion of either MLL2 or PRMT1 impairs cell migration and invasion.

Conclusions:

PRMT1-mediated methylation is a key mechanism for regulating MLL2 protein stability.
The MLL2-PRMT1 complex collectively regulates gene expression, impacting cellular functions critical for migration and invasion.