{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPHF6 plays a critical role in the pathogenesis of hematologic malignancies. In T‐cell acute lymphoblastic leukemia (T‐ALL) and acute myeloid leukemia (AML), loss‐of‐function mutations and deletions in this X‐linked gene predispose cells to oncogenic transformation, frequently in male patients, and are associated with aberrant expression of transcription factors and enhanced stem cell self‐renewal. Moreover, in mixed phenotype acute leukemia (MPAL) and other myeloid disorders, PHF6 lesions occur as early events that cooperate with additional genetic abnormalities to drive leukemia‐initiating cell activity, revealing a dual function that is both tumor‐suppressive and, in a lineage‐specific context, occasionally oncogenic."}, {"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": "\nGermline mutations in PHF6 underlie Borjeson‐Forssman‐Lehmann syndrome (BFLS), an X‐linked neurodevelopmental disorder marked by intellectual disability, distinctive facial features, and variable endocrine findings. The clinical spectrum extends beyond the classical description, with affected females often displaying overlapping features with Coffin–Siris syndrome as a consequence of skewed X‐inactivation and mosaicism. Variability in mutation type—from missense changes to truncations—leads to differences in protein stability and severity of neurodevelopmental impairment, which appears to be linked to PHF6’s role in regulating neuronal migration and transcription in the developing brain."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, PHF6 encodes a protein characterized by plant homeodomain (PHD)–like zinc finger motifs that direct its nucleoplasmic and nucleolar localization. It functions as a chromatin regulator by interacting with important epigenetic complexes—such as the NuRD complex—and by binding to double‐stranded DNA, thereby modulating transcription through promoter repression. In addition, PHF6 participates in the control of ribosomal RNA synthesis by interacting with transcription factors like UBF, influences cell cycle progression, and contributes to the DNA damage response via promotion of non–homologous end joining. Altered expression of PHF6 has also been implicated in solid tumors (for example, in endometrial and hepatocellular carcinoma), and studies using a PHF6‐derived tau peptide have provided insights into its relevance in tau aggregation and Alzheimer’s disease. Collectively, these molecular interactions underscore the multifaceted roles of PHF6 in transcriptional regulation, epigenetic modification, and genomic stability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Pieter Van Vlierberghe, Teresa Palomero, Hossein Khiabanian, et al. 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