{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNEK7 has emerged as a critical signaling node in the innate immune response, notably as a key mediator of NLRP3 inflammasome assembly and activation. In multiple studies, NEK7 directly binds the leucine‐rich repeat domain of NLRP3, serving as a switch that couples cellular signals—such as mitochondrial reactive oxygen species and changes in redox status—to caspase‐1 activation, thereby promoting the processing of proinflammatory cytokines and pyroptosis. Notably, structural studies have revealed that NEK7 bridges adjacent NLRP3 subunits through bipartite interactions, while posttranslational modifications (for example, deglutathionylation by GSTO1‐1) finely tune this process. In pathological contexts ranging from inflammatory bowel disease and diabetic arterial disease to chronic prostatitis, aberrations in the NEK7‐NLRP3 axis contribute to excessive inflammation and tissue injury."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its inflammatory role, NEK7 is indispensable for proper cell division. It participates in multiple aspects of mitotic regulation including centrosomal recruitment, spindle assembly, and cytokinesis. NEK7 functions downstream of upstream mitotic kinases such as NEK9—and along with the closely related NEK6, it is implicated in ensuring robust spindle formation by localizing at spindle poles and promoting the accumulation of pericentriolar material. Detailed kinetic and structural analyses have revealed an autoinhibited conformation of NEK7 that is relieved through specific protein–protein interactions, often involving regulatory residues (for instance, Tyr97) and dimerization events. Disruption of NEK7 function by RNA interference or expression of altered mutants leads to defects ranging from compromised spindle organization and procentriole formation to delays in cell cycle progression, underscoring its essential role in mitosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical roles in inflammation and mitosis, NEK7 is also implicated in oncogenesis and cellular homeostasis. Epigenetic regulators such as WHSC1 and chaperones like UNC45A have been shown to modulate NEK7 expression in cancer cells, where its overexpression correlates with enhanced proliferation and metastatic potential in tumors such as head and neck squamous cell carcinoma and hepatocellular carcinoma. In oncogenic fusion contexts (for example, in EML4‐ALK lung cancers), NEK7 is recruited via interactions with NEK9 to stabilize microtubules and promote aggressive cell migration. Moreover, NEK7 phosphorylates key substrates involved in telomere protection and microtubule dynamics, further linking its activity to genomic integrity. MicroRNA-mediated regulation of NEK7 expression has also been reported, suggesting additional layers of control. Collectively, these findings position NEK7 as a multifaceted kinase at the crossroads of inflammation, cell cycle control, and tumor biology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hexin Shi, Ying Wang, Xiaohong Li, et al. 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