scholarly journals Nuclear Receptor-Binding Sites of Coactivators Glucocorticoid Receptor Interacting Protein 1 (GRIP1) and Steroid Receptor Coactivator 1 (SRC-1): Multiple Motifs with Different Binding Specificities

1998 ◽  
Vol 12 (2) ◽  
pp. 302-313 ◽  
Author(s):  
Xiu Fen Ding ◽  
Carol M. Anderson ◽  
Han Ma ◽  
Heng Hong ◽  
Rosalie M. Uht ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Nuclear Receptor ◽  
Receptor Binding ◽  
Binding Sites ◽  
Steroid Receptor ◽  
Interacting Protein ◽  
Steroid Receptor Coactivator

scholarly journals DNA Sequence Constraints Define Functionally Active Steroid Nuclear Receptor Binding Sites in Chromatin

Endocrinology ◽  
2017 ◽  
Vol 158 (10) ◽  
pp. 3212-3234 ◽  
Author(s):  
Laurel A Coons ◽  
Sylvia C Hewitt ◽  
Adam B Burkholder ◽  
Donald P McDonnell ◽  
Kenneth S Korach
Keyword(s):  
Dna Sequence ◽  
Nuclear Receptor ◽  
Receptor Binding ◽  
Binding Sites ◽  
Sequence Constraints

scholarly journals A domain of the even-skipped protein represses transcription by preventing TFIID binding to a promoter: repression by cooperative blocking.

1995 ◽  
Vol 15 (9) ◽  
pp. 4683-4693 ◽  
Author(s):  
R J Austin ◽  
M D Biggin
Keyword(s):  
Glucocorticoid Receptor ◽  
Rna Polymerase Ii ◽  
Receptor Binding ◽  
Binding Sites ◽  
In Vitro System ◽  
Cooperative Interactions ◽  
General Transcription Factors ◽  
Promoter Dna ◽  
Template Dna

We examined the mechanism by which the C-terminal 236 amino acids of the even-skipped protein (region CD) repress transcription. A fusion protein, CDGB, was created that contains region CD fused to the glucocorticoid receptor DNA binding domain. This protein repressed transcription in an in vitro system containing purified fractions of the RNA polymerase II general transcription factors, and repression was dependent upon the presence of high-affinity glucocorticoid receptor binding sites in the promoter. Repression by CDGB was prevented when the promoter DNA was preincubated with TFIID or TBP, whereas preincubation of the template DNA with CDGB prevented TFIID binding. Together, these results strongly imply that CDGB represses transcription by inhibiting TFIID binding, and further experiments suggested a mechanism by which this may occur. Region CD can mediate cooperative interactions between repressor molecules such that molecules bound at the glucocorticoid receptor binding sites stabilize binding of additional CDGB molecules to low-affinity binding sites throughout the basal promoter. Binding to some of these low-affinity sites was shown to contribute to repression. Further experiments suggested that the full-length eve protein also represses transcription by the same mechanism. We speculate that occupancy of secondary sites within the basal promoter by CDGB or the eve protein inhibits subsequent TFIID binding to repress transcription, a mechanism we term cooperative blocking.

scholarly journals Attenuation of Glucocorticoid Signaling through Targeted Degradation of p300 via the 26S Proteasome Pathway

2002 ◽  
Vol 16 (12) ◽  
pp. 2819-2827 ◽  
Author(s):  
Qiao Li ◽  
Anna Su ◽  
Jihong Chen ◽  
Yvonne A. Lefebvre ◽  
Robert J. G. Haché
Keyword(s):  
Gene Expression ◽  
Glucocorticoid Receptor ◽  
Sodium Butyrate ◽  
Steroid Receptor ◽  
26S Proteasome ◽  
Regulatory Control ◽  
Specific Gene ◽  
Control Of Gene Expression ◽  
Steroid Receptor Coactivator ◽  
Proteasome Pathway

Abstract The effects of acetylation on gene expression are complex, with changes in chromatin accessibility intermingled with direct effects on transcriptional regulators. For the nuclear receptors, both positive and negative effects of acetylation on specific gene transcription have been observed. We report that p300 and steroid receptor coactivator 1 interact transiently with the glucocorticoid receptor and that the acetyltransferase activity of p300 makes an important contribution to glucocorticoid receptor-mediated transcription. Treatment of cells with the deacetylase inhibitor, sodium butyrate, inhibited steroid-induced transcription and altered the transient association of glucocorticoid receptor with p300 and steroid receptor coactivator 1. Additionally, sustained sodium butyrate treatment induced the degradation of p300 through the 26S proteasome pathway. Treatment with the proteasome inhibitor MG132 restored both the level of p300 protein and the transcriptional response to steroid over 20 h of treatment. These results reveal new levels for the regulatory control of gene expression by acetylation and suggest feedback control on p300 activity.

scholarly journals Cannabinoid Receptor Interacting Protein 1a Competition with β-Arrestin for CB1 Receptor Binding Sites

2016 ◽  
Vol 91 (2) ◽  
pp. 75-86 ◽  
Author(s):  
Lawrence C. Blume ◽  
Theresa Patten ◽  
Khalil Eldeeb ◽  
Sandra Leone-Kabler ◽  
Alexander A. Ilyasov ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Cannabinoid Receptor ◽  
Cb1 Receptor ◽  
Interacting Protein
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