{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:33:52Z","timestamp":1779345232998,"version":"3.51.4"},"reference-count":40,"publisher":"Proceedings of the National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,6,11]]},"abstract":"<jats:p>\n            Transcriptional coactivators implicated in gene activation by the thyroid hormone receptor (TR) include members of the p160\/steroid receptor coactivator (SRC) family of proteins, p300, and the multisubunit TR-associated protein (TRAP)\/Mediator complex. We investigated the temporal recruitment of these cofactors to mammalian thyroid hormone (T3)-responsive promoters\n            <jats:italic>in vivo<\/jats:italic>\n            . We show that upon T3 treatment, TR recruits all three types of coactivators to specific promoters in at least two sequential steps: p160\/SRC proteins and p300 are recruited first and rapidly induce histone acetylation, followed by the recruitment of the TRAP\/Mediator complex. Interestingly, inhibition of histone deacetylase activity with trichostatin A elicited a more rapid promoter recruitment of the TRAP\/Mediator complex but not p160\/SRC proteins. T3-dependent gene expression assays indicate that all three coactivators are targeted to a promoter before significant activation occurs. These findings thus suggest that histone acetylation may be a prerequisite for TRAP\/Mediator recruitment and function at specific T3-responsive mammalian promoters.\n          <\/jats:p>","DOI":"10.1073\/pnas.122004799","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:46:49Z","timestamp":1027694809000},"page":"7934-7939","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":138,"title":["Ordered recruitment of histone acetyltransferases and the TRAP\/Mediator complex to thyroid hormone-responsive promoters\n            <i>in vivo<\/i>"],"prefix":"10.1073","volume":"99","author":[{"given":"Dipali","family":"Sharma","sequence":"first","affiliation":[{"name":"Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph D.","family":"Fondell","sequence":"additional","affiliation":[{"name":"Department 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