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.
|Number of pages||8|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 2017 Aug 4|
Bibliographical noteFunding 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.
© 2017, American Society for Biochemistry and Molecular Biology Inc. All rights reserved.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology