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Related Experiment Videos

[Structure and function of TRAP]

A Nakai1, A Nagasaka

  • 1Department of Internal Medicine, Fujita Health University School of Medicine.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|April 1, 1994
PubMed
Summary
This summary is machine-generated.

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Thyroid hormone receptor (THR) binding to DNA is enhanced by T3 receptor auxiliary protein (TRAP). Retinoid X receptors (RXRs) can act as TRAP, forming heterodimers with THR to modulate gene expression.

Area of Science:

  • Molecular Endocrinology
  • Nuclear Receptor Signaling

Context:

  • Thyroid hormone receptor (THR) binds to thyroid hormone response elements (TREs).
  • Cellular nuclear extracts were observed to enhance THR-TRE binding via electrophoretic mobility shift assays.
  • This enhancing protein was identified as T3 receptor auxiliary protein (TRAP).

Purpose:

  • To identify proteins that enhance thyroid hormone receptor (THR) binding to DNA.
  • To characterize the function and interactions of T3 receptor auxiliary protein (TRAP).

Summary:

  • Retinoid X receptors (RXRs) function as TRAP, forming heterodimers with THR through their ligand-binding domains.
  • TRAP-THR heterodimerization involves regions with leucine zipper-like heptad repeats, forming amphipathic alpha-helices.
  • The synergistic effect of RXR's ligand, 9-cis retinoic acid, on T3/THR-mediated transactivation is dependent on the specific TRE sequence.

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Impact:

  • TRAP, including RXRs, plays a crucial role in regulating thyroid hormone-mediated gene transcription.
  • Understanding TRAP function provides insights into the molecular mechanisms controlling thyroid hormone signaling.
  • This research potentially reveals new targets for therapeutic interventions related to thyroid hormone action.