{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNDEL1 plays a critical role in neurodevelopment by orchestrating multiple aspects of neuronal migration and cytoskeletal reorganization. It serves as an essential mediator in the DISC1–NDEL1 pathway during cortical development, ensuring proper neurite extension and the entry of newborn neurons into their target laminae, while also partnering with regulators such as LIS1 and katanin p60 to modulate microtubule dynamics. In addition, post‐translational modifications including S‐nitrosylation have been shown to fine‐tune NDEL1 activity to promote dendritic arborization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in neuronal migration, NDEL1 is pivotal for proper mitotic progression and chromosome segregation. It contributes to the regulation of kinetochore–microtubule attachments by interacting with proteins such as Cenp-F and Nde1, thereby ensuring accurate mitotic spindle assembly, centrosomal maturation, and timely cell-cycle progression. These functions are modulated by phosphorylation events—mediated by kinases such as Aurora-A and Cdk1—that control NDEL1’s subcellular localization and turnover."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the level of cytoplasmic dynein motor regulation, NDEL1 is an important modulator that both restrains and facilitates dynein activity. It can relieve the inhibitory effect of LIS1 on dynein motility and supports dynein-dependent transport processes such as the assembly of a lamin B spindle matrix and aggresome formation. Moreover, NDEL1’s dynamic interaction with dynein is influenced by its own phosphorylation state and additional roles in protein quality control, including the targeting of misfolded Gβ subunits for degradation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPost‐translational modifications of NDEL1—including precise phosphorylation events and palmitoylation—not only regulate its binding interactions with key partners (such as DISC1 and LIS1) but also modulate its intrinsic enzymatic (oligopeptidase) activities. These modifications, along with its newly uncovered self-oligomerization properties, contribute to the regulation of neuropeptide turnover and neurite outgrowth, underlining an enzymatic facet to its multifaceted role in neuronal differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic and clinical studies further highlight the relevance of NDEL1 in psychiatric disorders. Disruption of its normal interactions—particularly with DISC1—and aberrant enzymatic activities have been implicated in schizophrenia and related mental illnesses. Altered NDEL1 expression in patient blood and the formation of insoluble DISC1 aggregates that fail to bind NDEL1 may contribute to the pathophysiology of these conditions, suggesting that precise regulation of NDEL1 is critical for both neural development and adult brain function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yuji Ozeki, Toshifumi Tomoda, John Kleiderlein, et al. 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