{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPA2G4, also known as ErbB3‐binding protein 1 (Ebp1), is a multifunctional protein belonging to the proliferation‐associated 2G4 family. Structural studies using high‐resolution crystallography and cryo–electron microscopy have revealed that PA2G4 adopts a conserved “pita‐bread” fold reminiscent of methionine aminopeptidases, yet it lacks enzymatic activity. PA2G4 is found in both the cytoplasm and nucleolus, where its binding to mature 80S ribosomes and specific regions—such as the flexible tunnel exit and associated rRNA expansions—links it to the regulation of ribosome assembly and translational control. In addition, two splice isoforms exist (p48 and p42) that display distinct subcellular distributions and protein–interaction patterns, providing the structural basis for its context‐dependent functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer cells, PA2G4 plays dichotomous roles that depend on its isoform and the tissue context. The larger p48 isoform frequently acts as an oncogene by engaging in protein–protein interactions that stabilize key oncoproteins—for example, it binds MYCN in neuroblastoma to prevent its degradation, interacts with HDM2 to promote p53 ubiquitination, and associates with CDK2 to undergo activating phosphorylation. In contrast, the shorter p42 isoform exerts tumor‐suppressive functions by coupling with factors such as the p85 regulatory subunit of PI3K and promoting its degradation (often via adapter functions involving the FBXW7 or HSP70/CHIP ubiquitin ligase complexes). PA2G4 also modulates receptor signaling in hormone‐dependent cancers by inhibiting androgen receptor transactivation and by reducing levels of ErbB2, thereby contributing to altered cellular proliferation, invasion, and drug sensitivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "18"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in modulating oncogenic signaling pathways, PA2G4 contributes to the regulation of mRNA fate and translational responses. By binding double‐stranded RNA elements and associating with ribonucleoprotein complexes, it influences the stability and turnover of transcripts such as bcl‐2 and participates in general translation control by protecting eukaryotic initiation factor 2α from stress‐induced phosphorylation. PA2G4 also demonstrates antiviral properties through selective inhibition of influenza virus RNA polymerase, while in non–cancer settings it regulates neurite outgrowth and heterochromatin assembly during neural development. Furthermore, PA2G4 has been recognized as an immunogenic tumor antigen in colorectal cancer and modulates inflammatory signaling in conditions like ulcerative colitis. Finally, its involvement in cell adhesion, migration, and invasion—as seen in multiple myeloma and salivary adenoid cystic carcinoma—underscores the protein’s diverse impact on disease progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Massimo Squatrito, Monica Mancino, Maddalena Donzelli, et al. 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