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Differential regulation of SF-1-cofactor interactions

Johan Lund1, Bente Børud, Gunnar Mellgren

  • 1Department of Anatomy and Cell Biology, University of Bergen, Norway. johan.lund@astrazeneca.com

Endocrine Research
|January 18, 2003
PubMed

Insights

Protein kinase A differentially regulates steroidogenic factor-1 (SF-1) activity. PKA enhances p/CIP coactivator function while downregulating TIF2, impacting SF-1 dependent transcription in steroidogenic organs.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Gene Regulation

Background:

  • Steroidogenic factor-1 (SF-1) is an orphan nuclear receptor crucial for steroidogenic organ development and function.
  • SF-1 transcriptional activity is modulated by coactivators, including p160 family members like p/CIP and TIF2.
  • Protein kinase A (PKA) is a key signaling molecule involved in cellular responses.

Purpose of the Study:

  • To investigate the differential effects of PKA on the coregulatory function of p/CIP and TIF2 in SF-1 dependent transcription.
  • To elucidate the molecular mechanisms underlying PKA's influence on SF-1 transcriptional complexes.
  • To identify novel SF-1 interacting proteins.

Main Methods:

  • Yeast two-hybrid screening to identify SF-1 interacting proteins.
  • Reporter gene assays to measure SF-1 dependent transcriptional activity.
  • Western blotting to assess protein levels and PKA-mediated modifications.

Main Results:

  • PKA potentiates p/CIP-stimulated SF-1 dependent transcription.
  • PKA activation leads to selective downregulation of TIF2 protein levels.
  • Downregulation of TIF2 by PKA results in repression of its coactivator function for SF-1.
  • A novel zinc finger protein interacting with the SF-1 AF-2 domain was identified.

Conclusions:

  • PKA exerts differential control over SF-1 coactivators, enhancing p/CIP and repressing TIF2.
  • This differential regulation provides a mechanism for modulating SF-1 activity in response to PKA signaling.
  • The identification of a novel SF-1 interacting protein may reveal new regulatory pathways.

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