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Terminal differentiation program of skeletal myogenesis is negatively regulated by O-GlcNAc glycosylation

Mitsutaka Ogawa1, Hidenori Mizofuchi, Yuki Kobayashi

  • 1Department of Bioscience, Nagahama Institute of Bio-Science and Technology, Nagahama, Japan.

Biochimica Et Biophysica Acta
|November 8, 2011
PubMed
Abstract

Insights

O-Linked β-N-acetylglucosaminylation (O-GlcNAcylation) decreases during skeletal muscle cell differentiation. Inhibiting O-GlcNAcase blocks this decrease and myoblast fusion, revealing O-GlcNAcylation negatively regulates muscle cell terminal differentiation.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • O-Linked β-N-acetylglucosaminylation (O-GlcNAcylation) is a dynamic post-translational modification regulating diverse cellular functions.
  • Over 500 nucleocytoplasmic proteins are O-GlcNAcylated, impacting cell cycle, transcription, and glucose sensing.
  • While implicated in lineage-specific differentiation, O-GlcNAcylation's role in skeletal myogenesis remained unexplored.

Purpose of the Study:

  • To investigate the role of O-GlcNAcylation in skeletal myogenesis.
  • To determine how O-GlcNAcylation affects the differentiation of muscle precursor cells.

Main Methods:

  • Utilized mouse C2C12 myoblasts to study O-GlcNAcylation dynamics during differentiation.
  • Employed genetic and pharmacological inhibition of O-GlcNAcase to assess its impact on myogenesis.
  • Analyzed the expression of key myogenic regulatory factors.

Main Results:

  • Observed a significant decrease in O-GlcNAcylation levels during myogenesis, preceding myoblast fusion.
  • Inhibition of O-GlcNAcase prevented the O-GlcNAcylation decrease and blocked myoblast fusion.
  • Inactivation of O-GlcNAcase did not affect cell-cycle exit or survival but inhibited the expression of myogenin and Mrf4.

Conclusions:

  • O-GlcNAcylation negatively regulates the terminal differentiation program of skeletal myogenesis.
  • A decrease in O-GlcNAcylation appears crucial for muscle lineage cell differentiation, suggesting a common role in muscle development.

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