{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nStratifin (SFN), also known as 14‐3‐3σ, is a multifunctional adaptor protein that plays a central role in regulating cell cycle progression and maintaining genomic integrity. It is inducible by p53 following DNA damage, where it helps enforce the G2/M checkpoint by stabilizing p53—through mechanisms that include antagonizing Mdm2 function—and by mediating the nuclear export and degradation of key cell cycle regulators such as phosphorylated ΔNp63α. Structural studies have revealed that SFN forms preferential homodimers with unique ring‐ring and salt bridge interactions that generate a specialized ligand binding surface, thereby facilitating specific phosphoserine-dependent interactions with substrates including peptides derived from proteins such as YAP."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSFN is frequently inactivated in several human cancers through epigenetic mechanisms such as promoter CpG hypermethylation—a change observed in breast, prostate, ovarian, nasopharyngeal, colorectal and other carcinomas—which compromises its tumor‐suppressive functions. In parallel, SFN can be secreted by differentiated keratinocytes (often via exosomal pathways) and act in a paracrine fashion to stimulate matrix metalloproteinase expression in dermal fibroblasts, thereby modulating extracellular matrix turnover and contributing to wound healing and anti‐fibrogenic responses. Altered SFN expression, by DNA methylation or enhanced proteasomal degradation, has also been linked to disrupted hormone receptor and growth factor signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "11"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond cell cycle control and extracellular signaling, SFN exerts additional regulatory roles in oncogenesis. It modulates mitotic translation by directly binding translation initiation factors during mitosis, influences nuclear-cytoplasmic shuttling of key proteins such as cyclin B1 and the glucocorticoid receptor, and contributes to tumor metabolic reprogramming by enhancing degradation of oncogenic factors like c-Myc. Furthermore, structural insights have detailed its interactions with partners such as HSPB6 and YAP, reinforcing its importance in regulating signal transduction pathways, cell proliferation and stress responses. Loss or dysregulation of SFN has been associated with increased cell invasiveness and metastatic potential in various cancer models, while in some contexts its inducible expression drives proliferative responses via pathways such as that mediated by insulin-like growth factor-I. SFN expression patterns also appear to provide a useful biomarker for tumor phenotype and prognosis, although its absence in certain tissues (for example, in meningioma where it is not expressed) underscores its tissue-specific roles."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "35"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Paulette Mhawech "}, {"type": "b", "children": [{"type": "t", "text": "14-3-3 proteins--an update."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Res (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.cr.7290291"}], "href": "https://doi.org/10.1038/sj.cr.7290291"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15857577"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15857577"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Heng-Yin Yang, Yu-Ye Wen, Chih-Hsin Chen, et al. 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