{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xiao X"],"funding":["NIAID NIH HHS","National Institutes of Health"],"pagination":["559-574"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5789412"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["215(2)"],"pubmed_abstract":["Th9 cells are prominently featured in allergic lung inflammation, but the mechanism that regulates IL-9 induction in T helper cells remains poorly defined. Here we demonstrate that formation of super-enhancers (SEs) is critical in robust induction of IL-9 and that assembly of the <i>Il9</i> SEs in Th cells requires OX40-triggered chromatin acetylation. Mechanistically, we found that OX40 costimulation induces RelB expression, which recruits the histone acetyltransferase p300 to the <i>Il9</i> locus to catalyze H3K27 acetylation. This allows binding of the SE factor Brd4 to organize assembly of the SE complex, which in turn drives robust IL-9 expression and Th9 cell induction. Thus, Th9 cells are strongly induced upon OX40 stimulation, and disruption of SEs abolished Th9 cell induction in v"],"journal":["The Journal of experimental medicine"],"pubmed_title":["Guidance of super-enhancers in regulation of IL-9 induction and airway inflammation."],"pmcid":["PMC5789412"],"funding_grant_id":["R01 AI106200","R01AI106200","R01AI129906","R01 AI129906"],"pubmed_authors":["Dou Y","Li XC","Li J","Fan Y","Lan P","Zhang X","Xiao Y","Xiao X","Lou X","Minze L","Shi X"],"additional_accession":[]},"is_claimable":false,"name":"Guidance of super-enhancers in regulation of IL-9 induction and airway inflammation.","description":"Th9 cells are prominently featured in allergic lung inflammation, but the mechanism that regulates IL-9 induction in T helper cells remains poorly defined. Here we demonstrate that formation of super-enhancers (SEs) is critical in robust induction of IL-9 and that assembly of the <i>Il9</i> SEs in Th cells requires OX40-triggered chromatin acetylation. Mechanistically, we found that OX40 costimulation induces RelB expression, which recruits the histone acetyltransferase p300 to the <i>Il9</i> locus to catalyze H3K27 acetylation. This allows binding of the SE factor Brd4 to organize assembly of the SE complex, which in turn drives robust IL-9 expression and Th9 cell induction. Thus, Th9 cells are strongly induced upon OX40 stimulation, and disruption of SEs abolished Th9 cell induction in v","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2026-05-03T03:33:54.821Z","creation":"2019-06-06T18:51:22Z"},"accession":"S-EPMC5789412","cross_references":{"pubmed":["29339447"],"doi":["10.1084/jem.20170928"]}}