Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases

FASEB J. 2019 Nov;33(11):11640-11654. doi: 10.1096/fj.201901175R. Epub 2019 Aug 1.

Abstract

Impaired glycolysis has pathologic effects on the occurrence and progression of liver diseases, and it appears that glycolysis is increased to different degrees in different liver diseases. As an important post-translational modification, reversible lysine acetylation regulates almost all cellular processes, including glycolysis. Lysine acetylation can occur enzymatically with acetyltransferases or nonenzymatically with acetyl-coenzyme A. Accompanied by the progression of liver diseases, there seems to be a temporal and spatial variation between enzymatic and nonenzymatic acetylations in the regulation of glycolysis. Here, we summarize the most recent findings on the functions and targets of acetylation in controlling glycolysis in the different stages of liver diseases. In addition, we discuss the differences and causes between enzymatic and nonenzymatic acetylations in regulating glycolysis throughout the progression of liver diseases. Then, we review these new discoveries to provide the potential implications of these findings for therapeutic interventions in liver diseases.-Li, J., Wang, T., Xia, J., Yao, W., Huang, F. Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases.

Keywords: acetyl-CoA; acetyltransferase; glucose metabolism; progression; target.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism*
  • Escherichia coli Proteins / metabolism
  • Glycolysis / physiology*
  • Humans
  • Liver Diseases / metabolism*
  • Protein Processing, Post-Translational / physiology*

Substances

  • Escherichia coli Proteins
  • Acetyltransferases