The new role of poly (rC)-binding proteins as iron transport chaperones: Proteins that could couple with inter-organelle interactions to safely traffic iron.
Cytosolic iron transport
Iron chaperone
PCBP
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
04
05
2020
revised:
07
07
2020
accepted:
11
07
2020
pubmed:
18
7
2020
medline:
5
1
2021
entrez:
18
7
2020
Statut:
ppublish
Résumé
Intracellular iron transport is mediated by iron chaperone proteins known as the poly(rC)-binding proteins (PCBPs), which were originally identified as RNA/DNA-binding molecules. PCBPs assume a role as not only as cytosolic iron carriers, but also as regulators of iron transport and recycling. PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1. Both PCBP1 and PCBP2 possess iron-binding activity and form hetero/homo dimer complexes. These iron chaperones have a subset of non-redundant functions and regulate iron metabolism independently. This intracellular iron chaperone system mediated by PCBPs provide a transport "gateway" of ferrous iron that may potentially link with dynamic, inter-organelle interactions to safely traffic intracellular iron.
Sections du résumé
BACKGROUND
Intracellular iron transport is mediated by iron chaperone proteins known as the poly(rC)-binding proteins (PCBPs), which were originally identified as RNA/DNA-binding molecules.
SCOPE OF REVIEW
PCBPs assume a role as not only as cytosolic iron carriers, but also as regulators of iron transport and recycling. PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.
MAJOR CONCLUSIONS
Both PCBP1 and PCBP2 possess iron-binding activity and form hetero/homo dimer complexes. These iron chaperones have a subset of non-redundant functions and regulate iron metabolism independently.
GENERAL SIGNIFICANCE
This intracellular iron chaperone system mediated by PCBPs provide a transport "gateway" of ferrous iron that may potentially link with dynamic, inter-organelle interactions to safely traffic intracellular iron.
Identifiants
pubmed: 32679248
pii: S0304-4165(20)30197-5
doi: 10.1016/j.bbagen.2020.129685
pii:
doi:
Substances chimiques
DNA-Binding Proteins
0
Iron-Binding Proteins
0
PCBP1 protein, human
0
PCBP2 protein, human
0
RNA-Binding Proteins
0
Iron
E1UOL152H7
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
129685Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest None.