{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSP3 is a versatile, GC‐rich sequence–binding transcription factor that functions in a highly context‐dependent manner. In many studies it has been shown to act either as an activator or as a repressor of target genes involved in processes such as angiogenesis, cell proliferation, and apoptosis. For example, under conditions of oxidative stress and in tumor cells, enhanced binding of SP3 (often in cooperation with SP1) to proximal GC boxes is critical for the induction of genes such as vascular endothelial growth factor A and for modulation of hTERT transcription in normal versus cancer cells, underpinning roles in neovascularization and tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMechanistically, SP3’s activity is regulated by post‐translational modifications and interactions with cofactors. Its function can be switched from repression to activation by acetylation, as described for transforming growth factor–beta receptor gene regulation, and its isoforms—generated via alternative translation initiation—are subjected to SUMO modification that further influences promoter responsiveness. In addition, SP3 is shown to interplay with other transcription factors (including SP1, nuclear orphan receptors, and hormonal receptors) and chromatin remodelers such as histone deacetylases, thereby modulating the transcriptional output of genes such as Axl, dopamine transporter, and secretin in a promoter‐ and cell type–specific fashion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, SP3 plays key roles in disease‐relevant transcriptional regulation. In cancer models, for instance, SP3 downregulation by agents such as curcumin or by microRNAs alters the expression of genes (including COX‑2, survivin, and ABC transporters) involved in chemoresistance, tumor growth, and invasion. Similarly, in nonmalignant settings its balanced expression relative to SP1 is fundamental for controlling extracellular matrix components (such as type I and II collagen), ion transporter genes (e.g., NHE3 and ABCA1), and enzymes involved in steroid and cytokine signaling. SP3’s nuclear distribution and its cooperation with other factors such as HIF‑1 under hypoxia further underscore its multifaceted contributions to cellular homeostasis and stress responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "C Ghayor, C Chadjichristos, J F Herrouin, et al. 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