Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.

@article{Deed1996NuclearLA,
  title={Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.},
  author={Richard W. Deed and Suzanne Armitage and John D. Norton},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 39},
  pages={23603-6}
}
Members of the Id family of helix-loop-helix proteins function as negative regulators of DNA binding, E protein, helix-loop-helix transcription factors in the control of cell growth, differentiation, and development. By using transient transfection analysis of COS cells, we show that in the absence of its E protein target, the Id3 protein is localized exclusively to the cytoplasm/perinuclear region. Co-transfection with E protein (E47) results in nuclear translocation of the Id3 protein, a… CONTINUE READING