Cited by 170Iron Metabolism and DisordersNeurological diseases and metabolismTrace Elements in Health

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Iron Export through the Transporter Ferroportin 1 Is Modulated by the Iron Chaperone PCBP2

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Yanatori, Izumi, Richardson, Des R., Imada, Kiyoshi, Kishi, Fumio·2016·Journal of Biological Chemistry

DOI 10.1074/jbc.m116.721936PMC PMC5016129

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Abstract

Ferroportin 1 (FPN1) is an iron export protein found in mammals. FPN1 is important for the export of iron across the basolateral membrane of absorptive enterocytes and across the plasma membrane of macrophages. The expression of FPN1 is regulated by hepcidin, which binds to FPN1 and then induces its degradation. Previously, we demonstrated that divalent metal transporter 1 (DMT1) interacts with the intracellular iron chaperone protein poly(rC)-binding protein 2 (PCBP2). Subsequently, PCBP2 receives iron from DMT1 and then disengages from the transporter. In this study, we investigated the function of PCBP2 in iron export. Mammalian genomes encode four PCBPs (i.e. PCBP1-4). Here, for the first time, we demonstrated using both yeast and mammalian cells that PCBP2, but not PCBP1, PCBP3, or PCBP4, binds with FPN1. Importantly, iron-loaded, but not iron-depleted, PCBP2 interacts with FPN1. The PCBP2-binding domain of FPN1 was identified in its C-terminal cytoplasmic region. The silencing of PCBP2 expression suppressed FPN1-dependent iron export from cells. These results suggest that FPN1 exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process.

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Authors: Yanatori, I., Richardson, D. R., Imada, K., & Kishi, F.
Affiliations: Kawasaki Medical School (JP)
The University of Sydney (AU)
Corresponding author: Kishi, Fumio
ORCID: Yanatori, Izumi
Richardson, Des R.
Kishi, Fumio
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2016-08
Volume: 291
Issue: 33
Pages: 17303-17318
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m116.721936
PMC: PMC5016129
OpenAlex: W2426081542
Cited by: 170
References: 59
Citations by year: 2026: 16 · 2025: 20 · 2024: 15 · 2023: 20 · 2022: 17 · 2021: 18 · 2020: 16 · 2019: 13 · 2018: 18 · 2017: 15 · 2016: 2
FWCI: 15.23
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 1484 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Charles Sturt University Research Output (CRO) (submittedVersion, other-oa)
Griffith Research Online (submittedVersion, cc-by)
Funders: Ministry of Education, Culture, Sports, Science, and Technology (22591052)
Kawasaki Medical School (Research Project Grants 26–26, 27–50)
National Health and Medical Research Council (Senior Principal Research Fellowship and Project Grants)
Japan Agency for Medical Research and Development (Research Program on Hepatitis)
Japan Society for the Promotion of Science
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: ferroportin 1, PCBP2, iron export, iron chaperone, DMT1, hepcidin, protein-protein interaction, binding domain, iron homeostasis, macrophages, enterocytes
MeSH terms: Protein Domains, Ferroportin, Biological Transport, Active, Cell Line, Gene Expression Regulation, Humans, Iron, RNA-Binding Proteins, Molecular Chaperones, Cation Transport Proteins, Hepcidins

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Iron Export through the Transporter Ferroportin 1 Is Modulated by the Iron Chaperone PCBP2

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