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유전체 항상성 연구단
유전체 항상성 연구단
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The E3 ubiquitin ligase TRIM25 regulates adipocyte differentiation via proteasome-mediated degradation of PPARγ

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Title
The E3 ubiquitin ligase TRIM25 regulates adipocyte differentiation via proteasome-mediated degradation of PPARγ
Author(s)
Jae Min Lee; Sun Sil Choi; Yo Han Lee; Keon Woo Khim; Sora Yoon; Byung-gyu Kim; Dougu Nam; Pann-Ghill Suh; Kyungjae Myung; Jang Hyun Choi
Publication Date
2018-10
Journal
EXPERIMENTAL AND MOLECULAR MEDICINE, v.50, no.10, pp.135 -
Publisher
NATURE PUBLISHING GROUP
Abstract
Peroxisome proliferator-activated receptor gamma (PPARγ) is a ligand-dependent transcription factor that regulates adipocyte differentiation and glucose homeostasis. The transcriptional activity of PPARγ is regulated not only by ligands but also by post-translational modifications (PTMs). In this study, we demonstrate that a novel E3 ligase of PPARγ, tripartite motif-containing 25 (TRIM25), directly induced the ubiquitination of PPARγ, leading to its proteasome-dependent degradation. During adipocyte differentiation, both TRIM25 mRNA and protein expression significantly decreased and negatively correlated with the expression of PPARγ. The stable expression of TRIM25 reduced PPARγ protein levels and suppressed adipocyte differentiation in 3T3-L1 cells. In contrast, the specific knockdown of TRIM25 increased PPARγ protein levels and stimulated adipocyte differentiation. Furthermore, TRIM25-knockout mouse embryonic fibroblasts (MEFs) exhibited an increased adipocyte differentiation capability compared with wild-type MEFs. Taken together, these data indicate that TRIM25 is a novel E3 ubiquitin ligase of PPARγ and that TRIM25 is a novel target for PPARγ-associated metabolic diseases. © The Author(s) 2018
URI
https://pr.ibs.re.kr/handle/8788114/5160
ISSN
2092-6413
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
Files in This Item:
s12276-018-0162-6.pdfDownload

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