The ins and outs of iron: Escorting iron through the mammalian cytosol.
Chaperones
Ferritin
Iron
Non-heme enzymes
Journal
Free radical biology & medicine
ISSN: 1873-4596
Titre abrégé: Free Radic Biol Med
Pays: United States
ID NLM: 8709159
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
27
07
2018
revised:
04
10
2018
accepted:
05
10
2018
pubmed:
16
10
2018
medline:
15
2
2020
entrez:
16
10
2018
Statut:
ppublish
Résumé
Mammalian cells contain thousands of metalloproteins and have evolved sophisticated systems for ensuring that metal cofactors are correctly assembled and delivered to their proper destinations. Equally critical in this process are the strategies to avoid the insertion of the wrong metal cofactor into apo-proteins and to avoid the damage that redox-active metals can catalyze in the cellular milieu. Iron and zinc are the most abundant metal cofactors in cells and iron cofactors include heme, iron-sulfur clusters, and mono- and dinuclear iron centers. Systems for the intracellular trafficking of iron cofactors are being characterized. This review focuses on the trafficking of ferrous iron cofactors in the cytosol of mammalian cells, a process that involves specialized iron-binding proteins, termed iron chaperones, of the poly rC-binding protein family.
Identifiants
pubmed: 30321701
pii: S0891-5849(18)32167-1
doi: 10.1016/j.freeradbiomed.2018.10.411
pii:
doi:
Substances chimiques
Iron-Binding Proteins
0
Iron-Sulfur Proteins
0
Metalloproteins
0
Molecular Chaperones
0
Heme
42VZT0U6YR
Sulfur
70FD1KFU70
Iron
E1UOL152H7
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
112-117Informations de copyright
Published by Elsevier Inc.