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A new group of conserved coactivators that increase the specificity of AP-1 transcription factors.

The Jun proteins are nuclear proteins that combine with Fos proteins to form a gene-regulatory protein, AP-1. They have highly conserved DNA-binding and dimerization domains, resulting in almost identical sequence-recognition properties. Nevertheless, there are many indications that each Jun protein activates a distinct and only partially overlapping set of AP-1 target genes. Using the more variable activation domain of c-Jun as a bait, we identified a protein, JAB1, that interacts with c-Jun and JunD, but not with JunB or v-Jun. As a result, JAB1 selectively potentiates transactivation by only c-Jun or JunD. In vitro, JAB1 specifically stabilizes complexes of c-Jun or JunD with AP-1 sites and does not affect binding of either JunB or v-Jun. The amino-terminal half of JAB1 is very similar to the amino terminal region of Pad1 from fission yeast, which was identified genetically as a coactivator of a subset of AP-1 target genes. JAB1 and Pad1 are also functionally interchangeable. They define a new group of coactivators that increase the specificity of target gene activation by AP-1 proteins.

Pubmed ID: 8837781


  • Claret FX
  • Hibi M
  • Dhut S
  • Toda T
  • Karin M



Publication Data

October 3, 1996

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Cell Line
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Peptide Hydrolases
  • Proto-Oncogene Proteins c-jun
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Trans-Activators
  • Transcription Factor AP-1
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation