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Transforming growth factor-beta-independent regulation of myogenesis by SnoN sumoylation

Katharine H Wrighton1, Min Liang, Brad Bryan

  • 1Michael E. DeBakey Department of Surgery and Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|January 5, 2007
PubMed

Insights

SnoN sumoylation at Lys-50 regulates muscle differentiation. This modification by PIAS1/PIASx enhances myogenesis by activating muscle-specific gene expression, revealing a new role for SUMOylation in cell development.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Oncoproteins c-Ski and SnoN regulate cellular transformation and TGF-beta signaling.
  • c-Ski/SnoN inhibit TGF-beta antiproliferative signals via Smad interaction.
  • The role of c-Ski/SnoN in myogenesis remains largely uncharacterized.

Purpose of the Study:

  • To biochemically characterize SnoN sumoylation.
  • To investigate the physiological function of SnoN sumoylation in myogenesis.
  • To explore the role of SUMO modification in myogenic differentiation.

Main Methods:

  • Biochemical characterization of SnoN sumoylation.
  • Identification of SUMO-protein isopeptide ligases (E3) for SnoN.
  • Analysis of muscle-specific gene expression and myotube formation in response to SnoN modification.

Main Results:

  • SnoN is sumoylated primarily at lysine 50 (Lys-50).
  • PIAS1 and PIASx proteins act as E3 ligases, stimulating SnoN sumoylation.
  • Loss of sumoylation at Lys-50 activates muscle-specific gene expression and enhances myotube formation.

Conclusions:

  • SnoN sumoylation at Lys-50 is a key regulator of myogenic differentiation.
  • SUMO modification provides a novel mechanism for controlling myogenesis.
  • This study uncovers a new function for SUMOylation in cellular development.

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