scholarly journals Identification and Characterization of the Alternatively Spliced Nuclear Receptor Coactivator-6 Isoforms

2011 ◽  
Vol 7 (5) ◽  
pp. 505-516 ◽  
Author(s):  
Qingtian Li ◽  
Jianming Xu
Keyword(s):  
Nuclear Receptor ◽  
Nuclear Receptor Coactivator ◽  
Alternatively Spliced ◽  
Identification And Characterization

scholarly journals ERAP140, a Conserved Tissue-Specific Nuclear Receptor Coactivator

2002 ◽  
Vol 22 (10) ◽  
pp. 3358-3372 ◽  
Author(s):  
Wenlin Shao ◽  
Shlomit Halachmi ◽  
Myles Brown
Keyword(s):  
Nuclear Receptor ◽  
Target Genes ◽  
Tissue Type ◽  
Interacting Proteins ◽  
Nuclear Receptor Coactivator ◽  
Nuclear Receptor Coactivators ◽  
The Brain ◽  
Identification And Characterization

ABSTRACT We report here the identification and characterization of a novel nuclear receptor coactivator, ERAP140. ERAP140 was isolated in a screen for ERα-interacting proteins using the ERα ligand binding domain as a probe. The ERAP140 protein shares no sequence and has little structural homology with other nuclear receptor cofactors. However, homologues of ERAP140 have been identified in mouse, Drosophila, and Caenorhabditis elegans. The expression of ERAP140 is cell and tissue type specific and is most abundant in the brain, where its expression is restricted to neurons. In addition to interacting with ERα, ERAP140 also binds ERβ, TRβ, PPARγ, and RARα. ERAP140 interacts with ERα via a noncanonical interaction motif. The ERα-ERAP140 association can be competed by coactivator NR boxes, indicating ERAP140 binds ERα on a surface similar to that of other coactivators. ERAP140 can enhance the transcriptional activities of nuclear receptors with which it interacts. In vivo, ERAP140 is recruited by estrogen-bound ERα to the promoter region of endogenous ERα target genes. Furthermore, the E2-induced recruitment of ERAP140 to the promoter follows a cyclic pattern similar to that of other coactivators. Our results suggest that ERAP140 represents a distinct class of nuclear receptor coactivators that mediates receptor signaling in specific target tissues.

Identification and characterization of alternatively spliced murine Rgs11 isoforms: genomic structure and gene analysis

2001 ◽  
Vol 94 (3-4) ◽  
pp. 216-224 ◽  
Author(s):  
A. Giudice ◽  
J.A. Gould ◽  
K.B. Freeman ◽  
S. Rastan ◽  
P. Hertzog ◽  
...  
Keyword(s):  
Genomic Structure ◽  
Gene Analysis ◽  
Alternatively Spliced ◽  
Identification And Characterization

scholarly journals Identification and characterization of two novel alternatively spliced E2F1 transcripts in the rat CNS

2018 ◽  
Vol 92 ◽  
pp. 1-11
Author(s):  
Dan P. Jackson ◽  
Jenhao H. Ting ◽  
Paul D. Pozniak ◽  
Claire Meurice ◽  
Stephanie S. Schleidt ◽  
...  
Keyword(s):  
Alternatively Spliced ◽  
Identification And Characterization ◽  
Rat Cns

scholarly journals PRIC295, a Nuclear Receptor Coactivator, Identified from PPAR-Interacting Cofactor Complex

PPAR Research ◽  
2010 ◽  
Vol 2010 ◽  
pp. 1-16 ◽  
Author(s):  
Sean R. Pyper ◽  
Navin Viswakarma ◽  
Yuzhi Jia ◽  
Yi-Jun Zhu ◽  
Joseph D. Fondell ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Target Genes ◽  
Peroxisome Proliferator ◽  
Dependent Manner ◽  
Peroxisome Proliferator Activated Receptor ◽  
Nuclear Receptor Coactivator ◽  
Evolutionarily Conserved

The peroxisome proliferator-activated receptor- (PPAR) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPAR in rodents leads to the development of hepatocellular carcinomas. The ability of PPAR to induce expression of its target genes depends on Mediator, an evolutionarily conserved complex of cofactors and, in particular, the subunit 1 (Med1) of this complex. Here, we report the identification and characterization of PPAR-interacting cofactor (PRIC)-295 (PRIC295), a novel coactivator protein, and show that it interacts with the Med1 and Med24 subunits of the Mediator complex. PRIC295 contains 10 LXXLL signature motifs that facilitate nuclear receptor binding and interacts with PPAR and five other members of the nuclear receptor superfamily in a ligand-dependent manner. PRIC295 enhances the transactivation function of PPAR, PPAR, and ER. These data demonstrate that PRIC295 interacts with nuclear receptors such as PPAR and functions as a transcription coactivator underin vitroconditions and may play an important role in mediating the effectsin vivoas a member of the PRIC complex with Med1 and Med24.

Identification and characterization of alternatively spliced variants of DNA methyltransferase 3a in mammalian cells

Gene ◽  
2002 ◽  
Vol 298 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Daniel J. Weisenberger ◽  
Mihaela Velicescu ◽  
Miguel A. Preciado-Lopez ◽  
Felicidad A. Gonzales ◽  
Yvonne C. Tsai ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Dna Methyltransferase ◽  
Alternatively Spliced ◽  
Dna Methyltransferase 3A ◽  
Identification And Characterization

scholarly journals Cloning and Characterization of RAP250, a Novel Nuclear Receptor Coactivator

2000 ◽  
Vol 275 (8) ◽  
pp. 5308-5317 ◽  
Author(s):  
Françoise Caira ◽  
Per Antonson ◽  
Markku Pelto-Huikko ◽  
Eckardt Treuter ◽  
Jan-Åke Gustafsson
Keyword(s):  
Nuclear Receptor ◽  
Nuclear Receptor Coactivator

Expression and characterization of the ferritin binding domain of Nuclear Receptor Coactivator-4 (NCOA4)

2017 ◽  
Vol 1861 (11) ◽  
pp. 2710-2716 ◽  
Author(s):  
Magdalena Gryzik ◽  
Ayush Srivastava ◽  
Giovanna Longhi ◽  
Michela Bertuzzi ◽  
Alessandra Gianoncelli ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Binding Domain ◽  
Nuclear Receptor Coactivator
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