{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPCBP1 plays a central role in cellular iron homeostasis by functioning as a cytosolic iron chaperone. It directly binds iron and facilitates its delivery to ferritin, thereby promoting iron storage and ensuring proper metallation of cytosolic nonheme iron enzymes. In erythroid cells, for example, PCBP1 directly interacts with ferritin and other enzymes such as deoxyhypusine hydroxylase to enable proper iron flux—activities that are dynamically regulated by cellular iron availability. In addition, PCBP1’s iron‐chaperone function has been shown to be essential during red blood cell differentiation and in protecting cells from iron toxicity, a role that is distinct and separable from its nucleic acid–binding activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in iron metabolism, PCBP1 is a multifunctional RNA-binding protein that orchestrates various aspects of posttranscriptional gene regulation. It modulates mRNA stability, translation, and alternative splicing by binding to specific CU- or C-rich motifs within the untranslated regions of target transcripts. For instance, PCBP1 regulates the translation of oncogenic factors such as PRL-3, androgen receptor, and p21(WAF1), and acts as an RNA chaperone to remodel structured RNA elements during internal ribosome entry site (IRES)-mediated translation. Moreover, PCBP1 influences alternative polyadenylation and splicing decisions—including switching STAT3 isoforms from oncogenic to tumor-suppressive forms—and thereby exerts tumor-suppressive functions in diverse cancer types. Collectively, these activities underscore PCBP1’s capacity to fine-tune gene expression programs critical for cell cycle control, differentiation, and tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPCBP1 is also implicated in cellular responses to stress, viral infection, and the modulation of cancer-related alternative splicing events that impact metastasis and stemness. It can associate with viral RNA elements—as seen in picornavirus and enterovirus 71 models—to influence viral translation and replication, albeit with varying efficiencies relative to its paralog PCBP2. In conditions of oxidative stress, PCBP1 discriminates between moderately and severely oxidized RNA species, promoting apoptotic responses when damage is extensive. In cancer, aberrant regulation or mutation of PCBP1 has been linked to altered splicing patterns of key adhesion and signaling molecules (such as CD44 and integrin β1), increased stemness, and metastatic progression in malignancies including Burkitt lymphoma, gastric, pancreatic, and lung cancers. These multifaceted roles position PCBP1 as a pivotal intracellular checkpoint, integrating signals from metabolic, stress, and splicing regulatory pathways to modulate both normal cellular functions and disease processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Haifeng Shi, Krisztina Z Bencze, Timothy L Stemmler, et al. 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