Acetylation of nuclear hormone receptor superfamily members: Thyroid hormone causes acetylation of its own receptor by a mitogen-activated protein kinase-dependent mechanism

Role of Sirtuin 1 in the Regulation of Hepatic Gene Expression by Thyroid Hormone

“…It might either directly deacetylate TR␤, or alternatively, it is possible that SIRT1 acts as a bridging molecule to recruit other coactivators. Previous studies reported that TR␤ was acetylated and that this acetylation was associated with increased nuclear localization (47). A subsequent report found that TR␣ was acetylated by p300 and that this acetylation enhanced the activity of TR␣ (48).…”

Reprogramming of the SWI/SNF complex for co-activation or co-repression in prohibitin-mediated estrogen receptor regulation

“…We and others have recently established that histone acetylation status and acetylation modulating proteins (p300, HDAC1, and so on) are associated with E2F-mediated transcriptional regulation (Brehm et al, 1998(Brehm et al, , 1999aBrehm and Kouzarides, 1999;Morris et al, 2000;Wang et al, 2002a). p300 and HDAC1 have also been reported to play critical roles in regulation of ERmediated transcriptional activity (Hanstein et al, 1996;Margueron et al, 2004;Jeffy et al, 2005;Lin et al, 2005). Interestingly, it has been recently reported that Brg1 collaborates with histone acetylation modulators in regulating ER-mediated transcription.…”

Overlapping nongenomic and genomic actions of thyroid hormone and steroids

“…It requires binding by nuclear thyroid hormone receptor (TR) proteins of 3,5,3′-triiodo-L-thyronine (T 3 ) and the formation of transcriptionally active complexes with nuclear co-activator proteins such as p300 and steroid receptor coactivator-1 (SRC-1) [6]. The complexes bind to promoter regions of thyroid hormoneresponsive genes to promote mRNA transcription.…”