{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTransferrin receptor 2 (TFR2) is a type II transmembrane glycoprotein predominantly expressed in hepatocytes and erythroid precursors that functions primarily as a sensor of circulating iron. By binding diferric (holo) transferrin, TFR2 becomes stabilized at the protein level—a process that does not involve transcriptional up‐regulation but rather an extension of its half‐life—thereby enabling it to participate in iron sensing. In hepatocytes, TFR2 interacts with other key iron‐regulatory proteins such as HFE and, via distinct domains compared to transferrin receptor 1 (TfR1), forms complexes that modulate the transcription of hepcidin, the master hormone that negatively controls intestinal iron uptake. Disruption of TFR2 function, as observed in patients with TFR2 mutations, results in blunted hepcidin responses and consequently systemic iron overload (hemochromatosis type 3). In addition, genetic studies and genome‐wide association analyses have identified common variants in TFR2 that associate with altered serum iron parameters and erythrocyte traits."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central role in iron sensing, TFR2 also contributes to specialized intracellular iron handling. In erythroid cells, for instance, TFR2 forms complexes with the erythropoietin receptor and facilitates the transport of iron from lysosomes to mitochondria—a crucial step for hemoglobin synthesis. Moreover, a novel mitochondrial targeting sequence within TFR2 has been identified in dopaminergic neurons, suggesting that TFR2 can deliver transferrin‐bound iron directly to mitochondria and even to components of the respiratory complex, with potential implications in neurodegenerative disorders such as Parkinson’s disease. At the cellular level, holo‐transferrin binding favors TFR2 recycling over lysosomal degradation, and a soluble form of TFR2 generated through ectodomain cleavage may exert modulatory effects on hepcidin promoter activation. Collectively, these findings underscore the multifaceted role of TFR2 as a regulator of iron homeostasis—integrating iron sensing, intracellular trafficking, and signal transduction—with its dysfunction predisposing to iron overload disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "27"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Robert E Fleming, John R Ahmann, Mary C Migas, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Structural, functional, and tissue distribution analysis of human transferrin receptor-2 by murine monoclonal antibodies and a polyclonal antiserum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2002-01-0076"}], "href": "https://doi.org/10.1182/blood-2002-01-0076"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12393650"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12393650"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Aeisha D Robb, Maria Ericsson, Marianne Wessling-Resnick "}, {"type": "b", "children": [{"type": "t", "text": "Transferrin receptor 2 mediates a biphasic pattern of transferrin uptake associated with ligand delivery to multivesicular bodies."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00337.2004"}], "href": "https://doi.org/10.1152/ajpcell.00337.2004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15317665"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15317665"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Aeisha Robb, Marianne Wessling-Resnick "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of transferrin receptor 2 protein levels by transferrin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2004-06-2481"}], "href": "https://doi.org/10.1182/blood-2004-06-2481"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15319276"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15319276"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Martha B Johnson, Caroline A Enns "}, {"type": "b", "children": [{"type": "t", "text": "Diferric transferrin regulates transferrin receptor 2 protein stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2004-06-2477"}], "href": "https://doi.org/10.1182/blood-2004-06-2477"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15319290"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15319290"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Elizabeta Nemeth, Antonella Roetto, Giovanni Garozzo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepcidin is decreased in TFR2 hemochromatosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2004-08-3042"}], "href": "https://doi.org/10.1182/blood-2004-08-3042"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15486069"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15486069"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Tapasree Goswami, Nancy C Andrews "}, {"type": "b", "children": [{"type": "t", "text": "Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C600197200"}], "href": "https://doi.org/10.1074/jbc.C600197200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16893896"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16893896"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Uta Merle, Franziska Theilig, Evelyn Fein, et al. 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