{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPIM3 is an oncogenic serine/threonine kinase that is pivotal in controlling cell cycle progression and survival. It directly phosphorylates key regulatory proteins – for example, targeting the cyclin‐dependent kinase inhibitor p27Kip1 to induce its binding to 14–3–3 proteins, nuclear export, and subsequent proteasomal degradation. This action enables cells to overcome growth arrest and evade apoptosis, while oncogenic factors such as c–Myc further upregulate its expression through conserved promoter elements, underscoring its role in malignant transformation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its direct actions on cell cycle proteins, PIM3 integrates metabolic cues into proliferative signaling. Studies have shown that loss of all PIM kinases activates AMPK due to disturbed energy ratios, whereas restoration of PIM3 in deficient cells not only normalizes protein synthesis but also upregulates central metabolic regulators, including c–Myc and PGC–1α, thereby promoting cell growth."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPIM3 overexpression is a recurrent feature in hepatocellular and other solid tumors where it accelerates tumor progression and confers resistance to anticancer therapies. In liver models, heightened PIM3 expression augments hepatocyte proliferation following carcinogen challenge and promotes tumor neovascularization, partly through phosphorylation of pro–apoptotic proteins such as Bad. Similar mechanisms contribute to chemoresistance in pancreatic and related cancers, making PIM3 an attractive candidate for targeted inhibition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in solid tumor growth, PIM3 contributes to the dynamic interplay between viruses and their host. In herpesvirus infections, for example, PIM3 phosphorylates latency-associated proteins to reverse transcriptional repression and trigger viral reactivation, while in classical Hodgkin lymphoma its activity fosters immune evasion through modulation of immunoregulatory proteins."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA multitude of studies across diverse cancer types further emphasize the broad oncogenic functions of PIM3. Its elevated expression correlates with aggressive tumor phenotypes, enhanced invasion, angiogenesis, and poor patient prognosis in settings such as pancreatic, prostate, ovarian, colorectal cancers, and melanoma. PIM3 exerts these effects by interacting with various signaling cascades – including those mediated by transcriptional regulators, microRNAs, and partner proteins – thereby reinforcing its central contribution to cell survival, metastasis, and therapeutic resistance. Collectively, these findings position PIM3 not only as a critical mechanistic driver of tumorigenesis but also as a promising biomarker and target for innovative anticancer therapies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Daisuke Morishita, Ryohei Katayama, Kazuhisa Sekimizu, et al. 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