Transcriptional regulation by steroid hormones

TL;DR: A greater understanding is required of the mechanisms by which glucocorticoids exert their anti-inflammatory and immunosuppressive actions, and recent research is shedding new light on some of these mechanisms and has produced some surprising new findings.

TL;DR: This review pays particular attention to the current knowledge and important results on the mechanisms of nongenomic steroid action and the modes of action are discussed in relation to their potential physiological or pathophysiological relevance and with regard to a cross-talk between genomic and nongnomic responses.

TL;DR: Evidence is presented for and against both the participation of classic receptors, or proteins closely related to them, as well as for the involvement of yet poorly understood, novel membrane steroid receptors.

TL;DR: Dual FRAP experiments show that fluorescent ER and SRC-1 exhibit similar dynamics only in the presence of E2, and in contrast to reports that several nuclear proteins show uniform dynamics, ER exhibits differential mobility depending upon several factors that are linked to its transcription function.

TL;DR: It is shown that glucocorticoids are potent inhibitors of nuclear factor kappa B activation in mice and cultured cells, mediated by induction of the IκBα inhibitory protein, which traps activated NF-κB in inactive cytoplasmic complexes.

TL;DR: A nuclear receptor co-repressor (N-CoR) of relative molecular mass 270K has been identified which mediates ligand-independent inhibition of gene transcription by these receptors, suggesting that the molecular mechanisms of repression by thyroid-hormone and retinoic-acid receptors are analogous to the co- repressor-dependent transcriptional inhibitory mechanisms of yeast and Drosophila.

TL;DR: It is proposed that CBP may participate in cAMP-regulated gene expression by interacting with the activated phosphorylated form of CREB, which is activated as a result of phosphorylation by protein kinase A7.

TL;DR: The phosphorylation of the human estrogen receptor (ER) serine residue at position 118 is required for full activity of the ER activation function 1 (AF-1), which is modulated by the phosphorylated Ser118 through the Ras-MAPK cascade of the growth factor signaling pathways.