Nuclear envelope-localized EGF family protein amphiregulin activates breast cancer cell migration in an EGF-like domain independent manner.

@article{Tanaka2012NuclearEE,
  title={Nuclear envelope-localized EGF family protein amphiregulin activates breast cancer cell migration in an EGF-like domain independent manner.},
  author={H. Tanaka and Yu Nishioka and Y. Yokoyama and S. Higashiyama and N. Matsuura and Shuji Matsuura and M. Hieda},
  journal={Biochemical and biophysical research communications},
  year={2012},
  volume={420 4},
  pages={
          721-6
        }
}
Amphiregulin (AREG), an EGF family protein, is synthesized as a type I transmembrane precursor (proAREG) and expressed on the cell surface with an extracellular EGF-like domain and an intracellular short cytoplasmic tail. The ectodomain shedding yields a soluble EGF receptor ligand (soluble AREG) which binds to EGF receptor (EGFR) and concomitantly induces migration of unshed proAREG from the plasma membrane to the nuclear envelope (NE). AREG is known to play a potential role in breast cancer… Expand
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