{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMetastasis‐associated protein 1 (MTA1) is a multifunctional nuclear regulator that serves as a core component of chromatin‐remodeling complexes—most notably the nucleosome remodeling and deacetylase (NuRD) complex. Structural studies have revealed that MTA1 wraps around class I histone deacetylases (HDACs) to form catalytic cores that precisely target nucleosomes, thereby modulating histone acetylation and gene transcription. In these complexes, MTA1 not only scaffolds essential proteins such as RBBP4 but also distinguishes its role from related family members (e.g., MTA2), enabling differential recruitment of cofactors and transcription regulators including oncogenic transcription factors like c‐MYC and developmental proteins such as HIC1. This dual capacity to both repress and activate transcription underpins its role in regulating hormone receptor signaling (e.g., estrogen receptor) and hypoxia‐inducible pathways.<br>."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMTA1 overexpression is a recurrent feature in a wide array of human cancers—including breast, prostate, ovarian, lung, colorectal, and hepatic carcinomas—and is closely associated with aggressive phenotypes. Elevated MTA1 levels promote malignant transformation by enhancing epithelial‐to‐mesenchymal transition (EMT), stimulating cellular migration and invasion, and modulating pro‐angiogenic pathways. Its activity is intricately linked to the repression of E‐cadherin (often via p‐AKT signaling) and the modulation of hormone receptor function. Furthermore, MTA1 is subject to post‐transcriptional regulation by various noncoding RNAs such as microRNAs (e.g. miR‑125b, miR‑543, and miR‑661) and circular RNAs that function as sponges to alter its expression. In doing so, MTA1 not only contributes to therapy resistance (for instance, tamoxifen resistance in breast cancer) but also serves as a robust prognostic indicator, correlating with higher tumor grade, metastasis, and poorer clinical outcomes across disease models.\n<br>."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional layers of regulation further refine MTA1’s functions. Post‐translational modifications—including ubiquitination, acetylation, and methylation—govern its protein stability and activity, as exemplified by COP1‐mediated degradation and dynamic switches that alter MTA1’s association with corepressor versus coactivator complexes. Through such mechanisms, MTA1 modulates DNA damage responses (for example, by repressing p21^WAF1 expression independent of p53) and influences cellular processes in non‐cancerous contexts such as spermatogenesis and retinal development. Moreover, MTA1 can be released in exosomes, thereby impacting the tumor microenvironment and serving as a biomarker for aggressive disease behavior. These diverse regulatory modes underscore MTA1’s role as a master “hub” in both cancer development and other pathological as well as physiological processes.\n<br>."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "30", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christopher J Millard, Peter J Watson, Ivana Celardo, et al. 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