The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.

@article{Welcker2004TheFT,
  title={The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.},
  author={Markus Welcker and Amir Orian and Jianping Jin and Jonathan E. Grim and J Wade Harper and Robert N. Eisenman and Bruce E. Clurman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 24},
  pages={9085-90}
}
Myc proteins regulate cell growth and division and are implicated in a wide range of human cancers. We show here that Fbw7, a component of the SCF(Fbw7) ubiquitin ligase and a tumor suppressor, promotes proteasome-dependent c-Myc turnover in vivo and c-Myc ubiquitination in vitro. Phosphorylation of c-Myc on threonine-58 (T58) by glycogen synthase kinase 3 regulates the binding of Fbw7 to c-Myc as well as Fbw7-mediated c-Myc degradation and ubiquitination. T58 is the most frequent site of c-myc… CONTINUE READING
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