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Related Experiment Videos

Human thyroid receptor forms tetramers in solution, which dissociate into dimers upon ligand binding.

Ana C M Figueira1, Sandra M G Dias, Maria A M Santos

  • 1Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil.

Cell Biochemistry and Biophysics
|May 9, 2006
PubMed
Summary

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Thyroid hormone receptors (TRs) can form tetramers, similar to retinoid X receptors (RXRs). Hormone binding causes these TR tetramers to dissociate into dimers, suggesting a new regulatory mechanism for TR activity.

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Biochemistry

Background:

  • Thyroid hormone receptors (TRs) and retinoid X receptors (RXRs) are nuclear receptors that regulate gene transcription.
  • TRs typically function as heterodimers with RXR or as homodimers/monomers.
  • RXR is known to form homodimers and homotetramers, with tetramerization potentially sequestering inactive receptors.

Purpose of the Study:

  • To investigate the multimeric state of a recombinant human TRbeta1 truncation (hTRbeta1deltaAB) in solution.
  • To determine if TRs, like RXRs, can form homotetramers.
  • To explore the influence of protein concentration and ligand binding on TR multimerization.

Main Methods:

  • Native gel electrophoresis
  • Chemical crosslinking

Related Experiment Videos

  • Gel filtration
  • Dynamic light scattering

    • Main Results:

    • hTRbeta1deltaAB exists as a mixture of monomers, dimers, and tetramers in solution.
    • Higher protein concentrations favor the formation of TR tetramers.
    • Binding of thyroid hormone induces dissociation of tetramers into dimers.

    Conclusions:

    • This study provides the first evidence that apo-thyroid hormone receptors can form homotetramers.
    • TR homotetramerization represents a novel regulatory mechanism for controlling TR activity.
    • The capacity for homotetramer formation may be a common feature among nuclear receptors.