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P4HB UFMylation regulates mitochondrial function and oxidative stress.

Jing Zhu1, Xirui Ma1, Yu Jing1

  • 1Department of Endocrinology and Metabolism, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Free Radical Biology & Medicine
|June 26, 2022
PubMed
Summary

This study identifies P4HB as a new target for UFMylation, a crucial post-translational modification. Disrupting P4HB UFMylation in liver cells leads to protein degradation, cellular stress, and potential implications for non-alcoholic fatty liver disease.

Keywords:
Mitochondrial functionOxidative stressP4HBUFM1UFMylationUbiquitination

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • UFMylation is a ubiquitin-like post-translational modification.
  • Few UFMylation targets have been identified to date.
  • P4HB protein possesses oxidoreductase, chaperone, and isomerase functions.

Purpose of the Study:

  • To identify new UFMylation targets.
  • To investigate the role of P4HB UFMylation in hepatocellular cells.
  • To explore the link between P4HB UFMylation and non-alcoholic fatty liver disease (NAFLD).

Main Methods:

  • Identification of P4HB as a novel UFMylation target.
  • Generation of a stable HepG2 cell line with defective P4HB UFMylation.
  • Analysis of cellular responses to P4HB UFMylation defects, including protein degradation, mitochondrial function, and stress responses.

Main Results:

  • P4HB is mono-UFMylated at three lysine residues.
  • Defective P4HB UFMylation promotes protein degradation via the ubiquitin-proteasome pathway.
  • Impaired P4HB UFMylation leads to mitochondrial dysfunction, oxidative stress, and ER stress in HepG2 cells, exacerbated by palmitic acid treatment.

Conclusions:

  • UFMylation is essential for maintaining P4HB stability and function in HepG2 cells.
  • P4HB UFMylation is a critical factor in cellular homeostasis.
  • P4HB UFMylation represents a potential therapeutic target for NAFLD.