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 in | Biochimica et biophysica acta. General subjects Vol. 1864; no. 11; p. 129685 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.11.2020
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Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 1872-8006 1872-8006 |
DOI | 10.1016/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. |
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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 |
Author_xml | – sequence: 1 givenname: Izumi surname: Yanatori fullname: Yanatori, Izumi organization: Department of Pathology and Biological Responses, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan – sequence: 2 givenname: Des R. surname: Richardson fullname: Richardson, Des R. organization: Department of Pathology and Biological Responses, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan – sequence: 3 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 – sequence: 4 givenname: Fumio surname: Kishi fullname: Kishi, Fumio email: fkishi-ygc@umin.ac.jp organization: Kenjinkai Healthcare Corporation, Japan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32679248$$D View this record in MEDLINE/PubMed |
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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 |
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