{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNuclear receptor corepressor 1 (NCOR1) serves as a pivotal scaffold in diverse transcriptional repression complexes that modulate nuclear receptor–mediated gene regulation. By directly binding to unliganded or aberrantly fused receptors, NCOR1 couples with histone deacetylases (particularly HDAC3) to maintain a hypo‐acetylated chromatin state and suppress transcription. This mechanism is employed in multiple contexts – for example, NCOR1 is exported from the nucleus in response to interleukin‐1β to derepress select NF‑κB targets (12150997), and it is hijacked by oncogenic fusions such as AML1/ETO to inhibit hematopoietic differentiation (9724795). In addition, NCOR1 is recruited by factors including Rev‑erbα to regulate circadian gene expression (15761026), by unliganded thyroid hormone receptors and their partners to mediate transcriptional repression (12861000), and by the androgen receptor (AR) to counterbalance coactivators during both agonist‐ and antagonist–mediated signaling (15598662; 16373395; 12089345). NCOR1 also plays a role in repressing transcription downstream of SUMOylated peroxisome proliferator–activated receptors (18832723; 19955185) and interacts within larger complexes that connect transcription with pre‑mRNA processing (12077342; 20581824)."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n \nDisruption of normal NCOR1 function or its mis‐directed recruitment can influence cell cycle control, differentiation, and tumorigenesis. NCOR1 is coopted by proteins such as THAP7 (15561719) and the scaffold attachment factors SAFB1/2 to mediate estrogen receptor repression (16195251), and its aberrant activity can distort peroxisome proliferator–activated receptor signaling in prostate cancer cells (20466759; 11903058). Moreover, interactions with chromatin‐modifying partners like JMJD2A (16024779) and associations with oncogenic fusion proteins such as PML–RARα (16730330) highlight its central role in transcriptional misregulation in acute leukemia (24315104; 21987803). Additional studies demonstrate that NCOR1 contributes to estrogen receptor–mediated down‑regulation of target genes (22944139), participates in mechanisms underlying tamoxifen resistance via competition with coactivators (27375289), and is essential for effective recruitment by AR antagonists (18852122)."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "28"}]}, {"type": "t", "text": "\n \nBeyond its classical role in nuclear receptor–dependent repression, NCOR1 is subject to multifaceted epigenetic modulation and post‑translational control that further fine‑tune gene expression and impact clinical outcomes. In VDR/RXR heterodimers, for example, NCOR1 is recruited in an agonist‑dependent manner to modulate calcium transport and immune functions (18362166), while in reproductive tissues hyperandrogenism is linked to aberrant NCOR1 expression that contributes to ovarian dysfunction (22622808). The stability and activity of NCOR1 can be regulated by deubiquitinating factors such as USP44 (27880911) or by critical functional domains (15695367), and its depletion has been associated with enhanced tumor invasiveness and metastasis (26729869). Furthermore, oncogenic viruses exploit NCOR1 by tethering it to viral fusion proteins (20181716) and its dynamic turnover is linked to proteolytic systems that affect mitochondrial gene expression (21143702; 21131350; 25928846). Emerging evidence also implicates circular RNAs derived from the NCOR1 locus in the regulation of TGF‑β–SMAD signaling and cancer metastasis (35395674), while studies on cofactor coding variants point to potential impacts on breast cancer risk (15377655; 18669643; 19183483; 26968201)."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sung Hee Baek, Kenneth A Ohgi, David W Rose, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Mammalian PRP4 kinase copurifies and interacts with components of both the U5 snRNP and the N-CoR deacetylase complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.22.14.5141-5156.2002"}], "href": "https://doi.org/10.1128/MCB.22.14.5141-5156.2002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12077342"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12077342"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Caroline A Phelan, Robert T Gampe, Millard H Lambert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of Rev-erbalpha bound to N-CoR reveals a unique mechanism of nuclear receptor-co-repressor interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.1860"}], "href": "https://doi.org/10.1038/nsmb.1860"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20581824"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20581824"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Todd Macfarlan, Sara Kutney, Brian Altman, et al. 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