{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTAF15 is a multifunctional RNA‐binding protein whose dysregulation plays a pivotal role in neurodegenerative diseases. Mutations or disease‐linked variants of TAF15 promote its mislocalization to the cytoplasm and subsequent aggregation, phenomena observed in amyotrophic lateral sclerosis (ALS) and certain forms of frontotemporal lobar degeneration. Studies have shown that mutant TAF15 forms cytoplasmic foci in motor neurons and, by aggregating in vitro, contributes to neurodegeneration. In addition, aberrant recruitment into stress granules or the formation of amyloid filaments further implicates TAF15 in the pathological cascades leading to neuronal cell death."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in neuropathology, TAF15 is central to RNA metabolism and regulation of gene expression. It participates in transcription by associating with components of the RNA polymerase II machinery, and directly engages in pre‐mRNA processing through its incorporation into distinct U1 small nuclear ribonucleoprotein (snRNP) complexes. Moreover, TAF15 is implicated in transcriptional activation events and is responsive to post‐translational modifications that modulate its nuclear localization and activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTAF15 also emerges as an important oncoprotein when its gene becomes fused with various transcription factors in hematological malignancies and soft tissue sarcomas. Fusion oncoproteins containing TAF15 not only deregulate normal transcriptional programs but also harness biomolecular condensate formation to aberrantly recruit RNA polymerase II and potentiate oncogenic transcriptional activation. In several studies, the expression and promoter strength of TAF15—and its role as a fusion partner—have been linked to tumorigenesis in leukemia, chondrosarcoma, and lung cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, TAF15 shows unique modes of regulation through post‐translational modifications and noncanonical RNA recognition. It is cleaved by executioner caspases at a defined consensus sequence, and its RNA recognition motif engages target RNAs via hydrogen‐bond networks rather than classical stacking interactions. Moreover, arginine methylation of its RGG repeats by PRMT1 influences its subcellular localization and gene regulatory functions, thereby fine‐tuning its participation in diverse nuclear processes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}, {"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, TAF15 interacts with various non‑coding RNAs and protein partners that further modulate mRNA stability and cellular signaling. In several contexts, long noncoding RNAs or circular RNAs recruit TAF15 to stabilize oncogenic mRNAs or regulatory transcripts, thereby influencing processes such as endothelial‐to‑mesenchymal transition, wound healing, and tumor progression. In addition, intrinsic differences in its cellular localization across cell types suggest that TAF15 may govern local RNA translation and transport in a context‑dependent manner."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "N Ticozzi, C Vance, A L Leclerc, et al. 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