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Chinese Journal of Clinical Pharmacology and Therapeutics ›› 2023, Vol. 28 ›› Issue (11): 1292-1298.doi: 10.12092/j.issn.1009-2501.2023.11.012

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Regulation mechanism of post-translational modification of farnesoid X receptor

LIU Zhaofeng1, LI Ling1, NA Shufang1, YUE Jiang2, YE Qifa1,3   

  1. 1Zhongnan Hospital of Wuhan University, Institute of Hepatobiliary Diseases of Wuhan University, Transplant Center of Wuhan University, Hubei Key Laboratory of Medical Technology on Transplantation, Wuhan 430071, Hubei, China; 2Department of Pharmacology, Basic Medical School of Wuhan University, Wuhan 430071, Hubei, China; 3The 3rd Xiangya Hospital of Central South University, Research Center of National Health Ministry on Transplantation Medicine Engineering and Technology, Changsha 410013, Hunan, China
  • Received:2023-06-05 Revised:2023-08-08 Online:2023-11-26 Published:2023-11-10

Abstract:

Farnesoid X receptor (FXR) is a nuclear receptor activated by bile acid that is involved in regulating gene expression related to bile acid, fat, glucose, and amino acid metabolism. The activity of FXR is regulated by a variety of post-translational modifications. Common post-translational modifications of FXR include O-GlcNAcylation, phosphorylation, acetylation,sumoylation, methylation, etc. These post-translational modifications may affect FXR binding of DNA and ligand, heterodimerization, and subcellular localization, and may specifically regulate downstream gene transcription and expression. Different post-translational modifications can lead to changes in FXR stability and biological function, which are closely related to the occurrence of diseases.This paper aims to review the post-translational modification of FXR in the past five years and the mechanisms involved in disease regulation, to explore the effects of post-translational modification on the physiological function of FXR and to provide a theoretical basis for mechanism research targeting FXR.

Key words: FXR, O-glycosylation, phosphorylation, acetylation, sumoylation, methylation

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