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. 2018 Mar 12;10:65. doi: 10.3389/fnagi.2018.00065

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Copyright © 2018 Ashraf, Clark and So.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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IRE/IRP regulation of ferritin and transferrin receptor. Proteins involved in the storage, export and uptake of iron are regulated via the interaction of iron-regulatory proteins (IRPs) with iron-responsive element (IREs), conserved RNA secondary structures (Rouault, 2006; Leipuviene and Theil, 2007). In conditions of low iron, IRP binds to a single IRE in the 5′-untranslated region (UTR) of ferritin mRNA to suppress their translation, while IRP binding to multiple IREs in the 3′ UTR of transferrin receptor-1 (TfR1) which stabilizes the mRNA for TfR1 synthesis. When the iron content in the cell is high, the lack of IRP-binding leads to increased synthesis of ferritin and destabilization of TfR1 mRNA.