Nuclear Receptor Coactivators: Mechanism and Therapeutic Targeting in Cancer

2020 ◽  
pp. 73-107
Author(s):  
Andrew Cannon ◽  
Christopher Thompson ◽  
Rakesh Bhatia ◽  
Sushil Kumar
Keyword(s):  
Nuclear Receptor ◽  
Therapeutic Targeting ◽  
Nuclear Receptor Coactivators

scholarly journals Hic-5, an adaptor-like nuclear receptor coactivator

2006 ◽  
Vol 4 (1) ◽  
pp. nrs.04019 ◽  
Author(s):  
Marjet D. Heitzer ◽  
Donald B. DeFranco
Keyword(s):  
Nuclear Receptor ◽  
Protein Complexes ◽  
Specific Protein ◽  
Nuclear Receptor Coactivator ◽  
Group Iii ◽  
Protein Protein Interaction ◽  
Direct Modification ◽  
Nuclear Receptor Coactivators ◽  
Multiple Protein ◽  
Receptor Interacting Proteins

In recent years, numerous nuclear receptor-interacting proteins have been identified that influence nuclear transcription through their direct modification of chromatin. Along with coactivators that possess histone acetyltransferase (HAT) or methyltransferase activity, other coactivators that lack recognizable chromatin-modifying activity have been discovered whose mechanism of action is largely unknown. The presence of multiple protein-protein interaction motifs within mechanistically undefined coactivators suggests that they function as adaptor molecules, either recruiting or stabilizing promoter-specific protein complexes. This perspective will focus on a family of nuclear receptor coactivators (i.e., group III LIM domain proteins related to paxillin) that appear to provide a scaffold to stabilize receptor interactions with chromatin-modifying coregulators.

The SRC family of nuclear receptor coactivators

Gene ◽  
2000 ◽  
Vol 245 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Christopher Leo ◽  
J.Don Chen
Keyword(s):  
Nuclear Receptor ◽  
Nuclear Receptor Coactivators

scholarly journals Nuclear Receptor Coactivators Modulate Hormone-Dependent Gene Expression in Brain and Female Reproductive Behavior in Rats

Endocrinology ◽  
2002 ◽  
Vol 143 (2) ◽  
pp. 436-444 ◽  
Author(s):  
Heather A. Molenda ◽  
Andreana L. Griffin ◽  
Anthony P. Auger ◽  
Margaret M. McCarthy ◽  
Marc J. Tetel
Keyword(s):  
Gene Expression ◽  
Nuclear Receptor ◽  
Reproductive Behavior ◽  
Nuclear Receptor Coactivators

scholarly journals Differential recruitment of nuclear receptor coactivators may determine alternative RNA splice site choice in target genes

2004 ◽  
Vol 101 (8) ◽  
pp. 2270-2274 ◽  
Author(s):  
D. Auboeuf ◽  
D. H. Dowhan ◽  
Y. K. Kang ◽  
K. Larkin ◽  
J. W. Lee ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Splice Site ◽  
Target Genes ◽  
Nuclear Receptor Coactivators

scholarly journals The DRIP Complex and SRC-1/p160 Coactivators Share Similar Nuclear Receptor Binding Determinants but Constitute Functionally Distinct Complexes

2000 ◽  
Vol 20 (8) ◽  
pp. 2718-2726 ◽  
Author(s):  
Christophe Rachez ◽  
Matthew Gamble ◽  
Chao-Pei Betty Chang ◽  
G. Brandon Atkins ◽  
Mitchell A. Lazar ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Receptor Binding ◽  
Transcriptional Activation ◽  
Thyroid Hormone Receptor ◽  
Nuclear Receptor Coactivators ◽  
Nuclear Extracts ◽  
Sequence Requirements

ABSTRACT Transcriptional activation requires both access to DNA assembled as chromatin and functional contact with components of the basal transcription machinery. Using the hormone-bound vitamin D3receptor (VDR) ligand binding domain (LBD) as an affinity matrix, we previously identified a novel multisubunit coactivator complex, DRIP (VDR-interacting proteins), required for transcriptional activation by nuclear receptors and several other transcription factors. In this report, we characterize the nuclear receptor binding features of DRIP205, a key subunit of the DRIP complex, that interacts directly with VDR and thyroid hormone receptor in response to ligand and anchors the other DRIP subunits to the nuclear receptor LBD. In common with other nuclear receptor coactivators, DRIP205 interaction occurs through one of two LXXLL motifs and requires the receptor's AF-2 subdomain. Although the second motif of DRIP205 is required only for VDR binding in vitro, both motifs are used in the context of an retinoid X receptor-VDR heterodimer on DNA and in transactivation in vivo. We demonstrate that both endogenous p160 coactivators and DRIP complexes bind to the VDR LBD from nuclear extracts through similar sequence requirements, but they do so as distinct complexes. Moreover, in contrast to the p160 family of coactivators, the DRIP complex is devoid of any histone acetyltransferase activity. The results demonstrate that different coactivator complexes with distinct functions bind to the same transactivation region of nuclear receptors, suggesting that they are both required for transcription activation by nuclear receptors.

Expression and regulation of nuclear receptor coactivators in glucocorticoid action

2002 ◽  
Vol 189 (1-2) ◽  
pp. 181-189 ◽  
Author(s):  
Isao Kurihara ◽  
Hirotaka Shibata ◽  
Toshihiko Suzuki ◽  
Takashi Ando ◽  
Sakiko Kobayashi ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Nuclear Receptor Coactivators ◽  
Glucocorticoid Action
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