Contribution of steroid receptor coactivator-1 and CREB binding protein in ligand-independent activity of estrogen receptor β

2001 ◽  
Vol 77 (1) ◽  
pp. 19-27 ◽  
Author(s):  
André Tremblay ◽  
Vincent Giguère
Keyword(s):  
Estrogen Receptor ◽  
Binding Protein ◽  
Steroid Receptor ◽  
Estrogen Receptor Β ◽  
Creb Binding Protein ◽  
Steroid Receptor Coactivator

scholarly journals Analysis of the Steroid Receptor Coactivator 1 (SRC1)-CREB Binding Protein Interaction Interface and Its Importance for the Function of SRC1

2001 ◽  
Vol 21 (1) ◽  
pp. 39-50 ◽  
Author(s):  
Hilary M. Sheppard ◽  
Janet C. Harries ◽  
Sagair Hussain ◽  
Charlotte Bevan ◽  
David M. Heery
Keyword(s):  
Binding Protein ◽  
Steroid Receptor ◽  
Creb Binding Protein ◽  
Interaction Domain ◽  
Steroid Receptor Coactivator ◽  
Helix Loop Helix ◽  
Rich Domain ◽  
Interaction Interface ◽  
Acetyltransferase Domain

ABSTRACT The transcriptional activity of nuclear receptors is mediated by coactivator proteins, including steroid receptor coactivator 1 (SRC1) and its homologues and the general coactivators CREB binding protein (CBP) and p300. SRC1 contains an activation domain (AD1) which functions via recruitment of CBP and and p300. In this study, we have used yeast two-hybrid and in vitro interaction-peptide inhibition experiments to map the AD1 domain of SRC1 to a 35-residue sequence potentially containing two α-helices. We also define a 72-amino-acid sequence in CBP necessary for SRC1 binding, designated the SRC1 interaction domain (SID). We show that in contrast to SRC1, direct binding of CBP to the estrogen receptor is weak, suggesting that SRC1 functions primarily as an adaptor to recruit CBP and p300. In support of this, we show that the ability of SRC1 to enhance ligand-dependent nuclear receptor activity in transiently transfected cells is dependent upon the integrity of the AD1 region. In contrast, the putative histone acetyltransferase domain, the Per-Arnt-Sim basic helix-loop-helix domain, the glutamine-rich domain, and AD2 can each be removed without loss of ligand-induced activity. Remarkably, a construct corresponding to residues 631 to 970, which contains only the LXXLL motifs and the AD1 region of SRC1, retained strong coactivator activity in our assays.

scholarly journals Nuclear Integration of Glucocorticoid Receptor and Nuclear Factor-κB Signaling by CREB-binding Protein and Steroid Receptor Coactivator-1

1998 ◽  
Vol 273 (45) ◽  
pp. 29291-29294 ◽  
Author(s):  
Kelly-Ann Sheppard ◽  
Kathleen M. Phelps ◽  
Amy J. Williams ◽  
Dimitris Thanos ◽  
Christopher K. Glass ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Binding Protein ◽  
Steroid Receptor ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Creb Binding Protein ◽  
Steroid Receptor Coactivator

scholarly journals Estrogen Receptor β Expression and Apoptosis of Spermatocytes of Mice Overexpressing a Rat Androgen-Binding Protein Transgene1

2004 ◽  
Vol 71 (5) ◽  
pp. 1461-1468 ◽  
Author(s):  
David M. Selva ◽  
Oscar M. Tirado ◽  
Nuria Toràn ◽  
Carlos A. Suárez-Quian ◽  
Jaume Reventos ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Binding Protein ◽  
Estrogen Receptor Β ◽  
Androgen Binding Protein ◽  
Androgen Binding

scholarly journals Ligand-Mediated Assembly and Real-Time Cellular Dynamics of Estrogen Receptor α-Coactivator Complexes in Living Cells

2001 ◽  
Vol 21 (13) ◽  
pp. 4404-4412 ◽  
Author(s):  
David L. Stenoien ◽  
Anne C. Nye ◽  
Maureen G. Mancini ◽  
Kavita Patel ◽  
Martin Dutertre ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Real Time ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Steroid Receptor ◽  
Estrogen Receptor Α ◽  
Living Cells ◽  
Live Cells ◽  
Creb Binding Protein ◽  
High Accumulation

ABSTRACT Studies with live cells demonstrate that agonist and antagonist rapidly (within minutes) modulate the subnuclear dynamics of estrogen receptor α (ER) and steroid receptor coactivator 1 (SRC-1). A functional cyan fluorescent protein (CFP)-taggedlac repressor-ER chimera (CFP-LacER) was used in live cells to discretely immobilize ER on stably integratedlac operator arrays to study recruitment of yellow fluorescent protein (YFP)-steroid receptor coactivators (YFP–SRC-1 and YFP-CREB binding protein [CBP]). In the absence of ligand, YFP–SRC-1 is found dispersed throughout the nucleoplasm, with a surprisingly high accumulation on the CFP-LacER arrays. Agonist addition results in the rapid (within minutes) recruitment of nucleoplasmic YFP–SRC-1, while antagonist additions diminish YFP–SRC-1–CFP-LacER associations. Less ligand-independent colocalization is observed with CFP-LacER and YFP-CBP, but agonist-induced recruitment occurs within minutes. The agonist-induced recruitment of coactivators requires helix 12 and critical residues in the ER–SRC-1 interaction surface, but not the F, AF-1, or DNA binding domains. Fluorescence recovery after photobleaching indicates that YFP–SRC-1, YFP-CBP, and CFP-LacER complexes undergo rapid (within seconds) molecular exchange even in the presence of an agonist. Taken together, these data suggest a dynamic view of receptor-coregulator interactions that is now amenable to real-time study in living cells.

Abstract 3104: Stapled peptide inhibitors of the estrogen receptor/steroid receptor coactivator interaction

2016 ◽  
Author(s):  
Terry W. Moore ◽  
Thomas E. Speltz ◽  
Sean W. Fanning ◽  
Christopher G. Mayne ◽  
Jonna Frasor ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Steroid Receptor ◽  
Peptide Inhibitors ◽  
Stapled Peptide ◽  
Steroid Receptor Coactivator
Sign in / Sign up

Export Citation Format

Share Document