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Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
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Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR

W Seol1, M J Mahon, Y K Lee

  • 1Department of Molecular Biology, Massachusetts General Hospital, Boston 02114, USA.

Molecular Endocrinology (Baltimore, Md.)
|December 1, 1996
PubMed

Insights

A new RIP13/N-CoR variant interacts with thyroid hormone receptor (TR) and retinoic acid receptor (RAR) via two distinct domains. This interaction, independent of repressor domains, highlights novel corepressor functions in nuclear hormone receptor regulation.

Area of Science:

  • Molecular Biology
  • Genetics
  • Endocrinology

Background:

  • Nuclear hormone receptors like thyroid hormone receptor (TR) and retinoic acid receptor (RAR) function as transcriptional repressors in ligand-unbound states.
  • This repression is mediated by corepressor proteins, including N-CoR, initially identified as a retinoid X receptor-interacting protein (RIP13).

Purpose of the Study:

  • To investigate a novel variant of RIP13/N-CoR lacking known repressor domains.
  • To characterize the interaction domains of this RIP13/N-CoR variant with TR and RAR.

Main Methods:

  • Yeast two-hybrid system
  • Mammalian two-hybrid system
  • Direct in vitro binding assays

Main Results:

  • A new RIP13/N-CoR variant was identified, structurally similar to SMRT/TRAC-2.
  • This variant possesses two distinct receptor interaction domains (ID-I and ID-II), both capable of independent binding to TR and RAR.
  • RIP13/N-CoR also interacts with retinoid X receptor, albeit with lower affinity compared to TR and RAR.

Conclusions:

  • RIP13/N-CoR interacts with multiple nuclear hormone receptors through two separate interaction domains.
  • The absence of repressor domains in this variant suggests alternative roles for corepressors.
  • Cell-type-specific factors may modulate corepressor function and nuclear hormone receptor activity.

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