Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells

Caroline C. Philpott, Moon Suhn Ryu, Avery Frey, Sarju Patel

Research output: Contribution to journalShort surveypeer-review

47 Scopus citations

Abstract

Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors. Iron cofactors include heme, iron–sulfur clusters, and simple iron ions. Poly(rC)-binding proteins are multifunctional adaptors that serve as iron ion chaperones in the cytosolic/nuclear compartment, binding iron at import and delivering it to enzymes, for storage (ferritin) and export (ferroportin). Ferritin iron is mobilized by autophagy through the cargo receptor, nuclear co-activator 4. The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chaperone complex. These proteins form a core system of cytosolic iron cofactor chaperones in mammalian cells.

Original languageEnglish (US)
Pages (from-to)12764-12771
Number of pages8
JournalJournal of Biological Chemistry
Volume292
Issue number31
DOIs
StatePublished - Aug 4 2017

Bibliographical note

Funding Information:
This work was supported by the Intramural Research Program of the NIDDK and the Office of Dietary Supplements, Office of the Director, National Institutes of Health. This is the fifth article in the Thematic Minireview series ?Metals in Biology 2017: Iron transport, storage, and the ramifications.? The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

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