Transactivation of LAP/NF-IL6 is mediated by an acidic domain in the N-terminal part of the protein.

@article{Cubero1995TransactivationOL,
  title={Transactivation of LAP/NF-IL6 is mediated by an acidic domain in the N-terminal part of the protein.},
  author={Francisco Javier Cubero and Denise L. Walker and J{\"o}rg Pl{\"u}mpe and Michael P. Manns},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 25},
  pages={15130-6}
}
LAP/NF-IL6 is a member of the C/EBP family of transcriptional activators and has been shown to be involved in the regulation of the acute-phase response. We have previously shown that phosphorylation of the liver-enriched transcriptional activator protein (LAP) Ser-105 enhances the activation of LAP-dependent genes. To identify the region which is important for gene activation, a series of LAP mutants were constructed, and domain swapping experiments with the DNA-binding domain of GAL4 were… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

Similar Papers

Loading similar papers…