Cited by 143Iron Metabolism and DisordersNeurological diseases and metabolismHemoglobin structure and function

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HFE and Transferrin Directly Compete for Transferrin Receptor in Solution and at the Cell Surface

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Giannetti, Anthony M., Björkman, Pamela J.·2004·Journal of Biological Chemistry

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Abstract

Transferrin receptor (TfR) is a dimeric cell surface protein that binds both the serum iron transport protein transferrin (Fe-Tf) and HFE, the protein mutated in patients with the iron overload disorder hereditary hemochromatosis. HFE and Fe-Tf can bind simultaneously to TfR to form a ternary complex, but HFE binding to TfR lowers the apparent affinity of the Fe-Tf/TfR interaction. This apparent affinity reduction could result from direct competition between HFE and Fe-Tf for their overlapping binding sites on each TfR polypeptide chain, from negative cooperativity, or from a combination of both. To explore the mechanism of the affinity reduction, we constructed a heterodimeric TfR that contains mutations such that one TfR chain binds only HFE and the other binds only Fe-Tf. Binding studies using a heterodimeric form of soluble TfR demonstrate that TfR does not exhibit cooperativity in heterotropic ligand binding, suggesting that some or all of the effects of HFE on iron homeostasis result from competition with Fe-Tf for TfR binding. Experiments using transfected cell lines demonstrate a physiological role for this competition in altering HFE trafficking patterns.

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Authors: Giannetti, A. M., & Björkman, P. J.
Affiliations: California Institute of Technology (US)
Corresponding author: Björkman, Pamela J.
ORCID: Björkman, Pamela J.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2004-06
Volume: 279
Issue: 24
Pages: 25866-25875
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m401467200
OpenAlex: W2009542872
Cited by: 143
References: 52
Citations by year: 2026: 5 · 2025: 4 · 2024: 1 · 2023: 6 · 2022: 5 · 2021: 6 · 2020: 7 · 2019: 6 · 2018: 5 · 2017: 4 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 6 · 2012: 7
FWCI: 6.71
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, 5981 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Funders: California Institute of Technology
National Institutes of Health
National Institute of General Medical Sciences (T32GM007616, 5T32-GM-7616)
National Institute of Diabetes and Digestive and Kidney Diseases (1 R01 DK60770, R01DK060770)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords: transferrin receptor, HFE gene, transferrin, hereditary hemochromatosis, iron homeostasis, ligand competition, ternary complex, negative cooperativity, protein trafficking, cell surface binding
MeSH terms: Hemochromatosis Protein, Binding, Competitive, Humans, Membrane Proteins, Receptors, Transferrin, Solutions, Transferrin, Histocompatibility Antigens Class I, Dimerization

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HFE and Transferrin Directly Compete for Transferrin Receptor in Solution and at the Cell Surface

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