{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMAP kinase‐interacting kinase 1 (MKNK1) is a crucial serine/threonine kinase that modulates mRNA translation through phosphorylation of eukaryotic initiation factor 4E (eIF4E). Multiple studies have demonstrated that MKNK1 integrates upstream signals from the MAPK, mTOR, PI3K, and AMPK pathways to fine‐tune cap‐dependent translation. For example, MKNK1 activity is induced in response to stimuli such as interferon‐γ or transforming growth factor‐β, leading to enhanced eIF4E phosphorylation that supports selective mRNA translation necessary for cell survival, differentiation, and inflammatory responses. In addition, MKNK1 phosphorylates substrates such as Sprouty2—thereby stabilizing its expression—and its splice variant MKNK1b exhibits higher basal catalytic activity compared with the full‐length isoform. These findings, together with RNA interference studies that implicate MNK regulation in the assembly of translation complexes, establish MKNK1 as a central mediator of translation initiation in diverse cellular contexts."}, {"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": "\nIn the context of human malignancies and pathological conditions, MKNK1‐mediated signaling plays an important role in tumor progression, drug resistance, and aberrant cell behavior. In glioblastoma, chronic myeloid leukemia, diffuse large B‐cell lymphoma, breast, prostate, melanoma, and nasopharyngeal carcinoma, overexpression or hyperactivation of MKNK1 correlates with increased eIF4E phosphorylation that drives oncogenic mRNA translation, fosters growth, and promotes metastasis. In several studies, pharmacologic inhibition of MKNK1 not only suppressed eIF4E phosphorylation and oncogenic protein synthesis (including cyclin D1, SMAD2, and EMT regulators) but also sensitized cancer cells to other therapeutic agents (for example, rapalogs or trastuzumab). Moreover, genetic association studies have linked MKNK1 with blood pressure phenotypes, and in airway smooth muscle cells, MKNK1 signaling contributes to chemokine production and cellular proliferation in asthma. Collectively, these findings support MKNK1 as a promising therapeutic target in diverse cancers and inflammatory diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "19"}, {"type": "fg_f", "ref": "9"}, {"type": "fg_fs", "start_ref": "20", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies have revealed roles for MKNK1 in viral infections, cell division, and metabolic regulation. MKNK1 activity influences viral replication by modulating internal ribosome entry site (IRES)‐mediated translation and, in some cases, facilitating viral entry. Upstream kinases such as Pak2 and AMPK regulate MKNK1 through direct phosphorylation events that alter its catalytic activity and subcellular localization, thereby affecting cytokinesis and cell abscission. In cell‐free systems and through RNA interference approaches, inhibition of MKNK1 has been shown to alter the composition of translation initiation complexes and impede efficient mRNA translation. Finally, MKNK1 is targeted by microRNAs—for example, miR‑370‑3p during adipogenesis—highlighting its involvement in lipid metabolism. These diverse functions underscore MKNK1’s pivotal role as a signaling node bridging external cues to the translational machinery."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Eric M Grund, Demetri D Spyropoulos, Dennis K Watson, et al. 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