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Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity.

The Fos/Jun and ATF/CREB families of transcription factors function in coupling extracellular signals to alterations in expression of specific target genes. Like many eukaryotic transcription factors, these proteins bind to DNA as dimers. Dimerization is mediated by a structure known as the "leucine-zipper" motif. Although Fos/Jun and ATF/CREB were previously thought to interact preferentially with different DNA regulatory elements (the AP-1/TRE and ATF/CRE sites, respectively), we find that members of these two families form selective cross-family heterodimers. The resulting heterodimers display distinguishable DNA binding specificities from each other and from their parental homodimers. These findings indicate that the Fos/Jun and ATF/CREB families of transcription factors are not as distinct as was previously thought. We suggest that they can be grouped into a superfamily of transcription factors.

Pubmed ID: 1827203


  • Hai T
  • Curran T


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

May 1, 1991

Associated Grants


Mesh Terms

  • Activating Transcription Factor 2
  • Base Sequence
  • Cyclic AMP Response Element-Binding Protein
  • DNA-Binding Proteins
  • In Vitro Techniques
  • Leucine Zippers
  • Macromolecular Substances
  • Molecular Sequence Data
  • Multigene Family
  • Oligonucleotides
  • Precipitin Tests
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-fos
  • Proto-Oncogene Proteins c-jun
  • Regulatory Sequences, Nucleic Acid
  • Structure-Activity Relationship
  • Transcription Factors