Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1.

@article{Brown1998NovelRO,
  title={Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1.},
  author={Nina M Brown and Sheila A. Anderson and David L. Steffen and Tami B. Carpenter and Mary Claire Kennedy and William E. Walden and Richard S. Eisenstein},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 26},
  pages={15235-40}
}
Animals regulate iron metabolism largely through the action of the iron regulatory proteins (IRPs). IRPs modulate mRNA utilization by binding to iron-responsive elements (IRE) in the 5' or 3' untranslated region of mRNAs encoding proteins involved in iron homeostasis or energy production. IRP1 is also the cytosolic isoform of aconitase. The activities of IRP1 are mutually exclusive and are modulated through the assembly/disassembly of its [4Fe-4S] cluster, reversibly converting it between an… CONTINUE READING