{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nYY1 functions as a pivotal architectural transcription factor that organizes higher‐order chromatin structure. It binds active enhancers and promoter‐proximal elements, often dimerizing to mediate long‐range enhancer–promoter loops and even engaging noncanonical DNA structures such as G-quadruplexes to facilitate unique chromatin contacts that regulate gene expression during cell fate transitions and neural lineage commitment."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various cancers, YY1 exerts context-dependent dual roles. On one hand, it can promote tumor progression by directly interacting with and facilitating the ubiquitination and destabilization of p53, repressing tumor-suppressor genes (such as APC) while simultaneously activating pathways like Wnt and c-Myc that drive cell proliferation and survival. Overexpression, as well as aberrant regulation of YY1, has been associated with increased oncogenic potential, enhanced cell growth, invasion and metastasis, and poorer clinical outcomes in colon, breast, prostate, and endometrial carcinomas."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its oncogenic roles, YY1 is essential for normal development and differentiation. It partners with chromatin-remodeling complexes such as INO80 and interacts with factors like HDAC1 to modulate diverse processes including viral gene silencing, TGF-β-induced differentiation, peripheral myelination, and even the initiation and maintenance of X-chromosome inactivation. Furthermore, aberrant YY1 dosage is linked to developmental syndromes characterized by cognitive impairment and congenital malformations."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nYY1’s activity is intricately controlled by posttranslational modifications and protein interactions. For example, glucose-dependent O-GlcNAcylation can prevent YY1 from binding partners like Rb, while S-nitrosation can impair its DNA-binding capacity. Additionally, through interactions with coactivators such as p300 and corepressors including HDAC3 and Mdm2, YY1 fine-tunes transcriptional outputs critical for cell cycle regulation and stress responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition, YY1 is embedded in complex regulatory networks involving noncoding RNAs and microRNAs. It regulates and is regulated by a spectrum of noncoding transcripts—modulating the transcription of oncogenic lncRNAs such as PVT1, assisting in circRNA-mediated signaling cascades via interactions with factors like DDX3, and being targeted by tumor-suppressive miRNAs (including miR-500a-5p, miR-34a, and miR-193a-5p). These interactions collectively contribute to the fine-tuning of gene expression programs driving tumor invasion, metastasis, and other malignant behaviors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, YY1 acts as a molecular integrator of transcription factor complexes. 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