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O-GlcNAcylation increases PYGL activity by promoting phosphorylation.

Yan-Fang Chen1, Jing-Jing Zhu1, Jing Li2

  • 1State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, 38 Xue Yuan Road, Beijing, 100191, China.

Glycobiology
|December 23, 2021
PubMed
Summary

O-GlcNAcylation of liver glycogen phosphorylase (PYGL) is crucial for cancer cell survival. This modification positively regulates PYGL enzymatic activity, impacting cancer pathophysiology.

Keywords:
O-GlcNAcylationenzyme activityglycogen metabolismliver glycogen phosphorylase (PYGL)phosphorylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • O-GlcNAcylation, a post-translational modification linking metabolism and signal transduction, is elevated in cancer cells.
  • Increased glycogen metabolism is observed in various tumors, indicating its role in cancer pathophysiology.
  • Liver glycogen phosphorylase (PYGL) is a key catabolic enzyme in glycogen metabolism.

Purpose of the Study:

  • To investigate the O-GlcNAcylation of liver glycogen phosphorylase (PYGL).
  • To understand the regulatory relationship between PYGL O-GlcNAcylation, phosphorylation, and enzymatic activity in the context of cancer.

Main Methods:

  • Expression and analysis of PYGL in HEK 293T and HCT116 cells.
  • Investigation of PYGL O-GlcNAcylation and phosphorylation (pSer15) under various metabolic conditions (glucose, insulin, glucagon, hypoxia).
  • Identification of O-GlcNAcylation sites and assessment of their impact on PYGL activity.

Main Results:

  • PYGL undergoes O-GlcNAcylation, with decreased modification under glucose/insulin and increased modification under glucagon/hypoxia.
  • Ser430 was identified as the major O-GlcNAcylation site, mutually reinforcing with pSer15.
  • Ser430 O-GlcNAcylation is essential for PYGL enzymatic activity, positively regulating pSer15.

Conclusions:

  • O-GlcNAcylation of PYGL positively regulates its pSer15 phosphorylation and enzymatic activity.
  • This study provides molecular insights into the post-translational regulation of PYGL in cancer.
  • O-GlcNAcylation of PYGL is a critical factor in cancer cell pathophysiology.