Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role.

@article{Sasaki2006SpatiotemporalRO,
  title={Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role.},
  author={Takanori Sasaki and Hirotada Kojima and Rikiya Kishimoto and Ayu Ikeda and Hiroyuki Kunimoto and Koich Nakajima},
  journal={Molecular cell},
  year={2006},
  volume={24 1},
  pages={
          63-75
        }
}
c-Fos is regulated by phosphorylation and multiple turnover mechanisms. We found that c-Fos was ubiquitylated in the cytoplasm during IL-6/gp130 stimulation under MEK inhibition and sought the mechanisms involved in the regulation. We show that sustained ERK5 activity and the E3 ligase UBR1 regulate the stability and subcellular localization of c-Fos. UBR1, rapidly induced by STAT3, interacts with and ubiquitylates c-Fos in the cytoplasm for its accelerated degradation. ERK5 inhibits the… CONTINUE READING