Changes in the content of steroid receptor coactivator-1 and silencing mediator for retinoid and thyroid hormone receptors in the rat brain during the estrous cycle

2005 ◽  
Vol 94 (1-3) ◽  
pp. 267-272 ◽  
Author(s):  
Ignacio Camacho-Arroyo ◽  
Teresa Neri-Gómez ◽  
Aliesha González-Arenas ◽  
Christian Guerra-Araiza
2004 ◽  
Vol 112 (5) ◽  
pp. 516-523 ◽  
Author(s):  
Kelly J Gauger ◽  
Yoshihisa Kato ◽  
Koichi Haraguchi ◽  
Hans-Joachim Lehmler ◽  
Larry W Robertson ◽  
...  

Thyroid ◽  
1991 ◽  
Vol 1 (2) ◽  
pp. 173-184 ◽  
Author(s):  
J. PUYMIRAT ◽  
M. MIEHE ◽  
R. MARCHAND ◽  
L. SARLIEVE ◽  
J.H. DUSSAULT

2001 ◽  
Vol 15 (7) ◽  
pp. 1170-1185 ◽  
Author(s):  
Zhihong Yang ◽  
Martin L. Privalsky

Abstract Thyroid hormone receptors (T3Rs) are hormone-regulated transcription factors that play important roles in vertebrate homeostasis, differentiation, and development. T3Rs are synthesized as multiple isoforms that display tissue-specific expression patterns and distinct transcriptional properties. Most T3R isoforms associate with coactivator proteins and mediate transcriptional activation only in the presence of thyroid hormone. The pituitary-specific T3Rβ-2 isoform departs from this general rule and is able to interact with p160 coactivators, and to mediate transcriptional activation in both the absence and presence of hormone. We report here that this hormone-independent activation is mediated by contacts between the unique N terminus of T3Rβ-2 and an internal interaction domain in the SRC-1 (steroid receptor coactivator-1) and GRIP-1 (glucocorticoid receptor interacting protein 1) coactivators. These hormone-independent contacts between T3Rβ-2 and the p160 coactivators are distinct in sequence and function from the LXXLL motifs that mediate hormone-dependent transcriptional activation and resemble instead a mode of coactivator recruitment previously observed only for the steroid hormone receptors and only in the presence of steroid hormone. Our results suggest that the transcriptional properties of the different T3R isoforms represent a combinatorial mixture of repression, antirepression, and hormone-independent and hormone-dependent activation functions that operate in conjunction to determine the ultimate transcriptional outcome.


Life Sciences ◽  
1999 ◽  
Vol 64 (20) ◽  
pp. 1793-1802 ◽  
Author(s):  
Chang-Gyu Hahn ◽  
Aaron C. Pawlyk ◽  
Peter C. Whybrow ◽  
Lazlo Gyulai ◽  
Shanaz M. Tejani-Butt

1978 ◽  
Vol 18 (3) ◽  
pp. 545-552 ◽  
Author(s):  
SINGARAM NAIDOO ◽  
THEONY VALCANA ◽  
PAOLA S. TIMIRAS

Endocrinology ◽  
1986 ◽  
Vol 118 (5) ◽  
pp. 1770-1776 ◽  
Author(s):  
TOSHIHIKO YOKOTA ◽  
HIROTOSHI NAKAMURA ◽  
TAKASHI AKAMIZU ◽  
TORU MORI ◽  
HIROO IMURA

2000 ◽  
Vol 856 (1-2) ◽  
pp. 119-128 ◽  
Author(s):  
Christophe Royer ◽  
Joël Lachuer ◽  
Gabriel Crouzoulon ◽  
Jean-Christophe Roux ◽  
Julie Peyronnet ◽  
...  

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