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SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells

Sung Wook Park1, Xinli Hu, Pawan Gupta

  • 1Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA.

Nature Structural & Molecular Biology
|December 26, 2006
PubMed

Insights

SUMOylation of the Tr2 nuclear receptor controls its function by altering coregulator binding and localization. This dynamic process fine-tunes Oct4 gene expression, regulating stem cell proliferation.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Gene Regulation

Background:

  • The Tr2 orphan nuclear receptor plays a role in gene regulation.
  • Tr2 interacts with coregulators and is localized to promyelocytic leukemia (Pml) nuclear bodies.

Purpose of the Study:

  • To investigate the role of SUMOylation in regulating Tr2 function.
  • To understand how Tr2's interaction with coregulators and its localization are affected by SUMOylation.

Main Methods:

  • SUMOylation assays
  • Co-immunoprecipitation
  • Immunofluorescence microscopy
  • Analysis of gene expression (Oct4)

Main Results:

  • SUMOylation of Tr2 at Lys238 leads to its release from Pml nuclear bodies.
  • SUMOylation induces an exchange of coregulators, with Rip140 replacing Pcaf.
  • This switch transforms Tr2 from an activator to a repressor of Oct4.
  • Tr2 exhibits dynamic partitioning between Pml-containing and Pml-free cellular compartments.

Conclusions:

  • SUMOylation-dependent partitioning and differential coregulator recruitment are key mechanisms controlling Tr2 activity.
  • These processes fine-tune Oct4 expression, impacting stem cell proliferation.

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