Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2
Open accessAbstract
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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Inside the enterocyte, Fe2+ is chaperoned to the basolateral surface by PCBP2 where it is released into the circulation for systemic use.
“Inside the enterocyte, Fe2+ iron is next chaperoned to the basolateral surface of the cell by PCBP2 (poly-(rC)-binding protein 2) where the iron is then released into the circulation for systemic use (Yanatori et al., 2016).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Yanatori et al., 2016
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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
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-08
- Volume
- 291
- Issue
- 33
- Pages
- 17303-17318
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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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