{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nFerroportin – the protein encoded by SLC40A1 – is the only known cellular iron exporter in vertebrates. It mediates the efflux of iron from diverse cell types (including duodenal enterocytes, macrophages, hepatocytes, and erythroid precursors) into plasma, thus playing a central role in systemic iron homeostasis. Its activity is tightly regulated by the peptide hormone hepcidin, which binds extracellularly to ferroportin and triggers a cascade of post‐translational events (including phosphorylation, ubiquitination and subsequent internalization and lysosomal degradation) that adjust iron export in response to iron loads and inflammation. Biochemical studies and state‐of‐the‐art cryogenic electron microscopy have elucidated the structure of ferroportin, identified distinct metal–binding sites, and even demonstrated its ability to transport additional divalent metals such as manganese, underscoring its substrate specificity. Moreover, accessory proteins, such as the iron chaperone PCBP2, have been shown to interact with ferroportin to facilitate the delivery of iron for export."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations in SLC40A1 cause a spectrum of iron‐loading disorders—often collectively termed “ferroportin disease” or non–HFE hemochromatosis. Many of these mutations diminish iron export activity either through a loss‐of‐function effect (resulting in iron sequestration in macrophages, hyperferritinemia with normal transferrin saturation, and even mild anemia) or by conferring resistance to hepcidin (which leads to unchecked iron export and subsequent parenchymal iron deposition). Such mutations have been identified in diverse populations and have been associated with variable clinical phenotypes, including familial presentations with autosomal dominant inheritance, altered immune microenvironments in hepatocellular carcinoma, and even modulated outcomes in cancer. Functional studies in cultured cells and Xenopus oocytes have characterized how specific missense substitutions or deletions impair proper membrane trafficking and hepcidin responsiveness, thereby disturbing the delicate balance of systemic iron flows."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in iron export, ferroportin is subject to complex regulation by multiple signaling pathways and microRNAs that modulate its transcription, translation, and turnover in a cell‐type– and context‐dependent manner. For example, oxidative stress and inflammatory mediators influence ferroportin expression in alveolar macrophages and other cells, with transcription factors such as Nrf2 playing pivotal roles in upregulating its mRNA levels. In addition, specific microRNAs have been identified that negatively regulate ferroportin expression in malignancies such as lung cancer and multiple myeloma, thereby contributing to intracellular iron accumulation that can drive cell proliferation and resistance to cell death. These findings highlight the multifaceted regulation of SLC40A1 and the diverse biological contexts—in inflammation, cancer, infection, and even degenerative disorders—in which ferroportin function is critical."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "36", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Andreas Rolfs, Herbert L Bonkovsky, James G Kohlroser, et al. 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