{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPCBP2 is a highly versatile RNA‐binding protein that regulates gene expression at multiple posttranscriptional levels. In nonviral contexts, it functions as an mRNA stability factor and modulator of translation, participates in alternative splicing and microRNA biogenesis, and even acts as an iron chaperone. PCBP2 receives and delivers ferrous iron to ferritin and other iron‐dependent enzymes, thereby contributing to cellular iron homeostasis. Structural studies of its KH domains have elucidated how PCBP2 specifically recognizes single‐stranded poly(C) sequences, including those present in telomeric regions, while its dynamic localization to stress granules and processing bodies underlines its role in remodeling mRNP complexes during cellular stress and in fine‐tuning miRNA processing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of viral infections, PCBP2 plays multifaceted roles that impact both the viral life cycle and the host antiviral response. It is essential for the initiation of translation on picornavirus genomes and for viral RNA replication, where virus‐encoded proteinases cleave PCBP2 to switch its function from promoting translation to facilitating replication. Furthermore, PCBP2 negatively regulates innate antiviral signaling by binding to key adaptor proteins such as MAVS and recruiting E3 ligases to trigger their proteasomal degradation. Its interactions have also been implicated in influencing the life cycles of hepatitis C, vesicular stomatitis, rabies, and Epstein–Barr viruses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies have further linked aberrant PCBP2 expression and activity to cancer and other pathologic processes. In various tumors—including gliomas, hepatocellular, pancreatic, and cervical cancers—PCBP2 is frequently upregulated and influences cell proliferation, apoptosis, drug resistance, and metastasis through stabilization or destabilization of specific mRNAs (for example, those encoding the androgen receptor, FHL3, STAT factors, c‐myc, and RRM1). In addition, PCBP2 can act as a decoy for regulatory proteins and is itself regulated by microRNAs such as miR‐214, thereby integrating oncogenic signals with posttranscriptional control. These insights underscore PCBP2’s role as a dynamic mediator in both normal cellular function and disease pathogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Bu B Yeap, Dominic C Voon, Julian P Vivian, et al. 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