The new role of poly (rC)-binding proteins as iron transport chaperones: Proteins that could couple with inter-organelle interactions to safely traffic iron

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...

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Published inBiochimica et biophysica acta. General subjects Vol. 1864; no. 11; p. 129685
Main Authors Yanatori, Izumi, Richardson, Des R., Toyokuni, Shinya, Kishi, Fumio
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.11.2020
Subjects
Online AccessGet full text
ISSN0304-4165
1872-8006
1872-8006
DOI10.1016/j.bbagen.2020.129685

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Abstract 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. •Intracellular iron is not found “free”, but is bound by iron chaperone proteins.•Iron chaperones include the multi-functional poly(rC)-binding proteins 1–4 (PCBPs).•PCBP1/2 play roles in iron metabolism, with the roles of PCBP3/4 being less clear.•The PCBPs bind 3 iron atoms and form hetero/homo dimer complexes.•PCBPs have a subset of non-redundant functions in iron metabolism.
AbstractList 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.
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.BACKGROUNDIntracellular 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.SCOPE OF REVIEWPCBPs 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.MAJOR CONCLUSIONSBoth 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.GENERAL SIGNIFICANCEThis 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.
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. •Intracellular iron is not found “free”, but is bound by iron chaperone proteins.•Iron chaperones include the multi-functional poly(rC)-binding proteins 1–4 (PCBPs).•PCBP1/2 play roles in iron metabolism, with the roles of PCBP3/4 being less clear.•The PCBPs bind 3 iron atoms and form hetero/homo dimer complexes.•PCBPs have a subset of non-redundant functions in iron metabolism.
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.
ArticleNumber 129685
Author Yanatori, Izumi
Toyokuni, Shinya
Richardson, Des R.
Kishi, Fumio
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  surname: Richardson
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  organization: Department of Pathology and Biological Responses, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan
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  givenname: Shinya
  surname: Toyokuni
  fullname: Toyokuni, Shinya
  organization: Department of Pathology and Biological Responses, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan
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  surname: Kishi
  fullname: Kishi, Fumio
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Keywords PCBP
Cytosolic iron transport
Iron chaperone
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Snippet Intracellular iron transport is mediated by iron chaperone proteins known as the poly(rC)-binding proteins (PCBPs), which were originally identified as...
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SubjectTerms Animals
Biological Transport
Cytosol - metabolism
Cytosolic iron transport
divalent metals
DNA-Binding Proteins - metabolism
ferritin
heme
heme oxygenase (biliverdin-producing)
Humans
iron
Iron - metabolism
iron absorption
Iron chaperone
Iron-Binding Proteins - metabolism
Models, Molecular
molecular chaperones
Organelles - metabolism
PCBP
RNA
RNA-Binding Proteins - metabolism
Title The new role of poly (rC)-binding proteins as iron transport chaperones: Proteins that could couple with inter-organelle interactions to safely traffic iron
URI https://dx.doi.org/10.1016/j.bbagen.2020.129685
https://www.ncbi.nlm.nih.gov/pubmed/32679248
https://www.proquest.com/docview/2424994739
https://www.proquest.com/docview/2477621032
Volume 1864
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