Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2.

@article{Domenico2009HepcidininducedIO,
  title={Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2.},
  author={Ivana De Domenico and Eric Lo and Diane M Ward and Jerry Kaplan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 10},
  pages={3800-5}
}
Hepcidin is a hormone secreted in response to iron loading and inflammation. Hepcidin binds to the iron exporter ferroportin, inducing its degradation and thus preventing iron entry into plasma. We determined that hepcidin binding to ferroportin leads to the binding and activation of the protein Janus Kinase2 (Jak2), which is required for phosphorylation of ferroportin. Ferroportin is a dimer and both monomers must be capable of binding hepcidin for Jak2 to bind to ferroportin. Once Jak2 is… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 63 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 30 references

Evidence for the multimeric structure of ferroportin

  • I De Domenico, DM Ward, G Musci, J Kaplan
  • Blood
  • 2007

Similar Papers

Loading similar papers…