{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMaternal embryonic leucine zipper kinase (MELK) is an AMPK‐related serine/threonine kinase that plays a crucial role in regulating cell cycle progression, proliferation, and apoptosis in both normal neural stem cells and a variety of malignant cells. Early studies have demonstrated that MELK is highly expressed in neural stem cells and is correlated with tumor grade and poor prognosis in aggressive brain tumors, as well as in transformed astrocytes and cancer stem cell populations. Its upregulation has been reported in glioblastoma, medulloblastoma, and other high‐grade brain tumors, suggesting that MELK is centrally involved in driving aberrant cell proliferation and tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional investigations have uncovered that MELK acts as a key signaling node by phosphorylating oncogenic transcription factors and substrates that influence cell survival, DNA damage repair, and therapy resistance. For example, in glioblastoma, MELK binds to FOXM1 and phosphorylates EZH2 to promote radioresistance while also regulating protein synthesis via phosphorylation of eukaryotic initiation factor 4B during mitosis. Moreover, genome‐editing and inhibitor studies have probed the functional dependency on MELK in various cancer cell lines—with some reports demonstrating that its inhibition (by small molecules such as OTSSP167 or novel compounds) suppresses growth, while others suggest context‐dependent or off‐target effects. These findings point to a complex role for MELK in mediating oncogenic signaling through pathways related to cell cycle control, translation regulation, and stress responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond central nervous system tumors, MELK is overexpressed in a wide range of human malignancies—including breast, ovarian, endometrial, gastric, lung, renal, and adrenocortical cancers—and its expression has been linked with aggressive tumor behavior, metastatic potential, and resistance to therapy. In these settings, MELK is implicated in the activation of oncogenic pathways such as AKT/mTOR and mTORC1 through phosphorylation of regulatory proteins like PRAS40, and in modulating cell migration via FAK/Src signaling. Structural studies have revealed that its catalytic domain is regulated by an ubiquitin‐associated region and redox-sensitive mechanisms, providing a framework for the rational design of MELK inhibitors which are currently under clinical investigation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Monique Beullens, Sadia Vancauwenbergh, Nick Morrice, et al. 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