Retinoic acid is a negative regulator of AP-1-responsive genes

Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6092-6. doi: 10.1073/pnas.88.14.6092.

Abstract

We present evidence that retinoic acid can down-regulate transcriptional activation by the nuclear protooncogene c-jun. All three members of the retinoic acid receptor (RAR) subfamily (RAR alpha, RAR beta, and RAR gamma) can repress transcriptional induction of the human collagenase gene or a heterologous promoter that contains the collagenase promoter AP-1-binding site. In contrast, the retinoid X receptor fails to repress Jun/AP-1 activity, demonstrating a significant difference between the two regulatory systems through which retinoids exert their transcriptional control. Analysis of RAR alpha mutants in transfection studies reveals that the DNA-binding domain is important for the inhibition of Jun/AP-1 activity, even though the RAR does not bind the collagenase AP-1 site. Rather, gel-retardation assays reveal that bacterially expressed full-length RAR alpha inhibits binding of Jun protein to target DNA. These data suggest that the RAR alpha may form a nonproductive complex with c-Jun and provides a simple mechanisms by which retinoic acid may limit cell growth and possibly malignant progression.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Line
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation, Enzymologic / drug effects
  • HeLa Cells / physiology
  • Microbial Collagenase / genetics*
  • Protein-Tyrosine Kinases / genetics
  • Proto-Oncogene Proteins c-jun
  • Proto-Oncogenes / drug effects*
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Transcription, Genetic / drug effects*
  • Transcriptional Activation / drug effects*
  • Transfection
  • Tretinoin / pharmacology*

Substances

  • DNA-Binding Proteins
  • Proto-Oncogene Proteins c-jun
  • Transcription Factors
  • Tretinoin
  • Protein-Tyrosine Kinases
  • Microbial Collagenase