ScholarWorks@숙명여자대학교

초록

The present study demonstrated that protein arginine methyltransferase 6 (PRMT6) negatively regulates the activity of peroxisome proliferator-activated receptor (PPAR). The results indicated that the overexpression of PRMT6 inhibited the transactivity of PPAR and subsequently decreased the expression levels of PPAR target genes. Contrarily, the depletion or inhibition of PRMT6 increased PPAR 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, PPAR. PRMT6 bound to the PPAR-responsive regulatory element of the adipocyte Protein 2 (aP2) promoter in conjunction with PPAR 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 PPAR activity in adipogenic differentiation and may be an attractive therapeutic target for human metabolic diseases.

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