The Journal of biological chemistry, 2017-08, Vol.292 (31), p.12764-12771
2017
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Details
- Autor(en) / Beteiligte
- Titel
- Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells
- Ist Teil von
- The Journal of biological chemistry, 2017-08, Vol.292 (31), p.12764-12771
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2017
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0021-9258eISSN: 1083-351XDOI: 10.1074/jbc.R117.791962Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5546017
- Format
- –
- Schlagworte
- Animals, Apoenzymes - chemistry, Apoenzymes - metabolism, Apoferritins - chemistry, Apoferritins - metabolism, Autophagy, BolA2, Carrier Proteins - chemistry, Carrier Proteins - metabolism, Cation Transport Proteins - chemistry, Cation Transport Proteins - metabolism, Cytosol - metabolism, Dimerization, DNA-Binding Proteins, Erythroid Precursor Cells - cytology, Erythroid Precursor Cells - metabolism, Ferritins - chemistry, Ferritins - metabolism, glutaredoxin, Heterogeneous-Nuclear Ribonucleoproteins - chemistry, Heterogeneous-Nuclear Ribonucleoproteins - metabolism, Humans, iron, Iron - metabolism, Iron-Sulfur Proteins - chemistry, Iron-Sulfur Proteins - metabolism, iron–sulfur protein, metalloprotein, Minireviews, Models, Biological, Models, Molecular, molecular chaperone, Molecular Chaperones - chemistry, Molecular Chaperones - metabolism, Nuclear Receptor Coactivators - chemistry, Nuclear Receptor Coactivators - metabolism, poly C-binding protein, Protein Multimerization, Protein Transport, Proteins - chemistry, Proteins - metabolism, RNA-Binding Proteins - chemistry, RNA-Binding Proteins - metabolism