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Updated: Jan 26, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
Protein arginine methyltransferase 6 suppresses adipogenic differentiation by repressing peroxisome
Jee Won Hwang1, Yun-Seong So1, Gyu-Un Bae1
1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul 140‑742, Republic of Korea.
Abstract:
The present study demonstrated that protein arginine methyltransferase 6 (PRMT6) negatively regulates the activity of peroxisome proliferator‑activated receptor γ (PPARγ). The results indicated that the overexpression of PRMT6 inhibited the transactivity of PPARγ and subsequently decreased the expression levels of PPARγ target genes. Contrarily, the depletion or inhibition of PRMT6 increased PPARγ reporter activity and the expression of its target genes. It was also confirmed that PRMT6 was involved in the process of adipocyte differentiation. In addition, PRMT6 interacted with, but did not methylate, PPARγ. PRMT6 bound to the PPAR‑responsive regulatory element of the adipocyte Protein 2 (aP2) promoter in conjunction with PPARγ and generated the repressive epigenetic mark arginine 2 on histone H3 asymmetric di‑methylation, which suppressed aP2 gene expression. Therefore, PRMT6 may serve as an important regulator of PPARγ activity in adipogenic differentiation and may be an attractive therapeutic target for human metabolic diseases.
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