Management versus miscues in the cytosolic labile iron pool: The varied functions of iron chaperones.
Ferroptosis
Glutathione
Iron chaperone
PCBP
Steatosis
Journal
Biochimica et biophysica acta. Molecular cell research
ISSN: 1879-2596
Titre abrégé: Biochim Biophys Acta Mol Cell Res
Pays: Netherlands
ID NLM: 101731731
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
30
06
2020
revised:
13
08
2020
accepted:
14
08
2020
pubmed:
25
8
2020
medline:
8
1
2021
entrez:
25
8
2020
Statut:
ppublish
Résumé
Iron-containing proteins rely on the incorporation of a set of iron cofactors for activity. The cofactors must be synthesized or assembled from raw materials located within the cell. The chemical nature of this pool of raw material - referred to as the labile iron pool - has become clearer with the identification of micro- and macro-molecules that coordinate iron within the cell. These molecules function as a buffer system for the management of intracellular iron and are the focus of this review, with emphasis on the major iron chaperone protein coordinating the labile iron pool: poly C-binding protein 1.
Identifiants
pubmed: 32835748
pii: S0167-4889(20)30188-9
doi: 10.1016/j.bbamcr.2020.118830
pmc: PMC7484093
mid: NIHMS1622625
pii:
doi:
Substances chimiques
DNA-Binding Proteins
0
Iron-Sulfur Proteins
0
Molecular Chaperones
0
PCBP1 protein, human
0
RNA-Binding Proteins
0
Iron
E1UOL152H7
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
118830Subventions
Organisme : Intramural NIH HHS
ID : Z01 DK054510
Pays : United States
Informations de copyright
Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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