| First Author | Philpott CC | Year | 2017 |
| Journal | J Biol Chem | Volume | 292 |
| Issue | 31 | Pages | 12764-12771 |
| PubMed ID | 28615454 | Mgi Jnum | J:247308 |
| Mgi Id | MGI:5915443 | Doi | 10.1074/jbc.R117.791962 |
| Citation | Philpott CC, et al. (2017) Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells. J Biol Chem 292(31):12764-12771 |
| abstractText | 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. |
