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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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Impaired Repressor Function in SUMOylation-Defective Thyroid Hormone Receptor Isoforms.

Joachim M Weitzel1

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European Thyroid Journal
|November 16, 2016
PubMed
Summary

Thyroid hormone receptor (TR) SUMOylation impacts gene transcription. Impaired SUMOylation reduces TR

Keywords:
Gene expressionLigand-dependent transcription factorPosttranslational modificationSUMOTransrepression

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Biology

Background:

  • Nuclear receptors, including thyroid hormone receptors (TRs), undergo posttranslational modifications.
  • TR transcriptional activity is influenced by thyroid hormones (T3 and T4) and posttranslational modifications.

Purpose of the Study:

  • To investigate the SUMOylation of TR isoforms.
  • To determine the effects of SUMOylation on TR transcriptional activity and promoter occupancy.

Main Methods:

  • In vitro SUMOylation assays of wild-type and mutant TR.
  • Chromatin immunoprecipitation (ChIP) and Re-ChIP analyses to assess TR and cofactor promoter occupancy.

Main Results:

  • Identified specific SUMOylation sites on TRα (K281, K387) and TRβ (K50, K443).
  • Demonstrated that TRs are targets for SUMO-1, -2, and -3 variants.
  • SUMOylation-defective TR mutants altered the transcription of T3-regulated genes.

Conclusions:

  • SUMOylation is crucial for TR's repressor function in the absence of T3.
  • SUMOylation affects TR interactions with cofactors like SRC-1 and NCoR.
  • TR SUMOylation fine-tunes transcriptional responses, impacting cellular and physiological homeostasis.