Please use this identifier to cite or link to this item: https://doi.org/10.3390/ijms19061738
Title: Functional regulation of PPARs through post-translational modifications
Authors: Brunmeir R.
Xu F. 
Keywords: Nuclear receptors; Post-translational modifications; PPAR?; PPAR?/?; PPAR?
Issue Date: 2018
Publisher: MDPI AG
Citation: Brunmeir R., Xu F. (2018). Functional regulation of PPARs through post-translational modifications. International Journal of Molecular Sciences 19 (6) : 1-16. ScholarBank@NUS Repository. https://doi.org/10.3390/ijms19061738
Abstract: Peroxisome proliferator-activated receptors (PPARs) belong to the nuclear receptor superfamily and they are essential regulators of cell differentiation, tissue development, and energy metabolism. Given their central roles in sensing the cellular metabolic state and controlling metabolic homeostasis, PPARs became important targets of drug development for the management of metabolic disorders. The function of PPARs is mainly regulated through ligand binding, which induces structural changes, further affecting the interactions with co-activators or co-repressors to stimulate or inhibit their functions. In addition, PPAR functions are also regulated by various Post-translational modifications (PTMs). These PTMs include phosphorylation, SUMOylation, ubiquitination, acetylation, and O-GlcNAcylation, which are found at numerous modification sites. The addition of these PTMs has a wide spectrum of consequences on protein stability, transactivation function, and co-factor interaction. Moreover, certain PTMs in PPAR proteins have been associated with the status of metabolic diseases. In this review, we summarize the PTMs found on the three PPAR isoforms PPAR?, PPAR?/?, and PPAR?, and their corresponding modifying enzymes. We also discuss the functional roles of these PTMs in regulating metabolic homeostasis and provide a perspective for future research in this intriguing field. © 2018 by the authors. Licensee MDPI, Basel, Switzerland.
Source Title: International Journal of Molecular Sciences
URI: http://scholarbank.nus.edu.sg/handle/10635/152511
ISSN: 16616596
DOI: 10.3390/ijms19061738
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