{"type": "root", "children": [{"type": "t", "text": "<div>\n "}, {"type": "p", "children": [{"type": "t", "text": "\n CHD9 is a member of the group III chromodomain‐helicase–DNA‐binding family of ATP‐dependent chromatin remodelers that appears to exert context‐dependent roles in transcriptional regulation. Biochemical analyses indicate that although its homologs (CHD6, CHD7, and CHD8) display distinct nucleosome‐remodeling specificities, CHD9 has emerged as an important regulator of chromatin structure in specialized cellular compartments (for instance, within the nucleolus), where a nucleolar isoform (n‐CHD9) associates with RNA polymerase I and other nucleolar factors to influence rRNA biogenesis and chromatin accessibility at rDNA loci."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition, CHD9 has been implicated in regulating gene expression programs that affect cell phenotype. In oral squamous cell carcinoma, experimental silencing of CHD9 (along with other targets) significantly accelerated cell invasion, suggesting that it may function as a negative regulator of invasive behavior."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Moreover, recurrent gene fusions involving CHD9–for example, as a partner in BCOR‐CHD9 fusions in a subset of soft tissue neoplasms–point to its involvement in aberrant transcriptional control that could contribute to tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n CHD9 is also highly expressed in specific developmental contexts. Its elevated expression in growing oocytes suggests roles in modulating chromatin looseness associated with pluripotency and the early steps of cell fate determination."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " In the context of glucocorticoid signaling, CHD9 is required at a subset of glucocorticoid receptor (GR)–binding sites where it cooperates with ATP‐dependent remodeling complexes to facilitate chromatin remodeling and robust GR occupancy; this activity is counteracted by the coregulator Hic‐5, which impedes GR access by selectively inhibiting CHD9 (and BRM) recruitment."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n Despite these nuanced roles in gene regulation and chromatin remodeling in various cell types, mouse knockout studies have shown that CHD9 is dispensable for overall development and viability, underscoring the highly context‐dependent and possibly redundant nature of its functions under normal physiological conditions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Collectively, these studies support a model in which CHD9 modulates chromatin structure at both the nucleolar level and at defined enhancer or promoter regions, thereby influencing transcriptional programs that contribute to cell differentiation and oncogenic processes.\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n (1)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "&nbsp; (2)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "&nbsp; (3)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "&nbsp; (4)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "&nbsp; (5)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "&nbsp; (6)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "&nbsp; (7)."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n</div>"}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ronit Salomon-Kent, Ronit Marom, Sam John, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Gene expression regulation by the Chromodomain helicase DNA-binding protein 9 (CHD9) chromatin remodeler is dispensable for murine development."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0233394"}], "href": "https://doi.org/10.1371/journal.pone.0233394"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32453735"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32453735"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Benjamin J Manning, Timur Yusufzai "}, {"type": "b", "children": [{"type": "t", "text": "The ATP-dependent chromatin remodeling enzymes CHD6, CHD7, and CHD8 exhibit distinct nucleosome binding and remodeling activities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M117.779470"}], "href": "https://doi.org/10.1074/jbc.M117.779470"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28533432"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28533432"}]}]}]}