{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTransforming acidic coiled‐coil protein 3 (TACC3) is a pivotal factor in ensuring proper mitotic progression. It plays a central role in mitotic spindle dynamics by mediating centrosome integrity, microtubule nucleation, and accurate chromosome segregation. TACC3 achieves these functions via interactions with key partners such as the microtubule polymerase ch‐TOG and the adaptor protein clathrin, and its spindle‐recruitment is tightly regulated by Aurora‐A kinase–dependent phosphorylation. Disruption of TACC3 function leads to defective kinetochore–microtubule attachments, aberrant spindle formation, and ultimately aneuploidy, while also affecting processes like central spindle assembly during anaphase and proper nuclear envelope organization."}, {"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": "\nIn addition to its canonical mitotic roles, aberrations involving TACC3 contribute directly to oncogenic signaling. Recurrent chromosomal translocations generate in‐frame fusions linking the fibroblast growth factor receptor (FGFR) kinase domains with the TACC3 coiled‐coil region. Such FGFR–TACC3 fusion proteins display constitutive kinase activity, leading to mitotic errors (and consequent aneuploidy), evasion of microRNA regulation, and acquired resistance to targeted inhibitors in cancers such as glioblastoma, bladder, nasopharyngeal, and non–small cell lung carcinomas. Structural investigations further reveal that the TACC3 coiled‐coil domain not only enforces mitotic functions but can, when fused, alter downstream signaling pathways that drive tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cell division, deregulated expression of TACC3 has been associated with tumor aggressiveness and poor prognosis in a variety of malignancies—including cervical, thyroid, breast, lung, hepatocellular, colorectal, esophageal, bladder, renal, and even osteosarcomas. In these contexts, TACC3 overexpression drives epithelial–mesenchymal transition (EMT) via activation of signaling cascades such as PI3K/Akt, ERK, and Wnt/β‐catenin, accelerates cell cycle progression through upregulation of E2F1, and disrupts DNA damage repair pathways, thereby promoting genomic instability. Moreover, its aberrant levels have been linked to the acquisition of cancer stem cell–like properties and altered therapeutic responses, marking TACC3 as both a promising prognostic biomarker and a candidate therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, the regulation of TACC3 itself is governed by complex mechanisms that control its protein stability, subcellular localization, and interaction dynamics. Regulatory inputs—including ubiquitin–proteasome pathways mediated by Cdh1 and associations with coactivators that bridge its mitotic and transcriptional roles—ensure that TACC3 activity is properly integrated into both spindle assembly and wider cellular signaling networks. Such finely tuned regulation is critical not only for normal cell division but also for the aberrant signaling events observed during tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Leonid Schneider, Frank Essmann, Anja Kletke, et al. 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