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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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CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 and inhibits its transactivation

Ki Cheol Park1, Kwang-Hoon Song, Hyo Kyun Chung

  • 1Laboratory of Endocrine Cell Biology, Department of Internal Medicine, Chungnam National University College of Medicine, 640 Daesadong Chungku Daejeon 301-721, Korea.

Molecular Endocrinology (Baltimore, Md.)
|October 2, 2004
PubMed

Insights

CR6-interacting factor 1 (CRIF1) is a nuclear protein that represses the orphan nuclear receptor Nur77. CRIF1 inhibits Nur77

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Nuclear Receptor Signaling

Background:

  • CRISPR-interacting factor 1 (CRIF1) is a nuclear protein involved in cell cycle regulation.
  • The specific nuclear functions of CRIF1 remain largely uncharacterized.

Purpose of the Study:

  • To investigate the role of CRIF1 as a coregulator of orphan nuclear receptor transactivation.
  • To elucidate the mechanism by which CRIF1 influences Nur77 activity.

Main Methods:

  • In vitro and in vivo interaction studies (e.g., co-immunoprecipitation).
  • Transient transfection assays to assess transactivation.
  • Small interfering RNA (siRNA) for gene silencing.
  • Analysis of promoter activity and cell cycle progression.

Main Results:

  • CRIF1 directly interacts with the Nur77 AB domain.
  • CRIF1 significantly inhibits Nur77 AB domain-mediated transactivation.
  • CRIF1 acts as an intrinsic repressor, independent of histone deacetylase activity.
  • CRIF1 represses Nur77-induced promoter activity and cell cycle progression.

Conclusions:

  • CRIF1 functions as a novel repressor of the orphan nuclear receptor Nur77.
  • CRIF1 inhibits Nur77 transcriptional activity through its AB domain.
  • CRIF1 plays a role in regulating Nur77-mediated cellular processes, including cell cycle progression.

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