The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers (Q44489701)

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English	The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

3 December 2017

The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers (English)

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

author name string

Maurizio Gianní

1

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Europe PubMed Central

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3 December 2017

Anne Tarrade

2

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Europe PubMed Central

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3 December 2017

Elisa Agnese Nigro

3

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Europe PubMed Central

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3 December 2017

Enrico Garattini

4

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Europe PubMed Central

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3 December 2017

Cécile Rochette-Egly

5

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Europe PubMed Central

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3 December 2017

language of work or name

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publication date

24 June 2003

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3 December 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

3 December 2017

278

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Europe PubMed Central

PubMed publication ID

3 December 2017

36

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

34458-34466

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

Orphan nuclear receptors: from gene to function

1 reference

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Structural studies on nuclear receptors.

1 reference

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21 January 2018

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains

1 reference

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21 January 2018

The nuclear receptor ligand-binding domain: structure and function

1 reference

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Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR.

1 reference

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Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications

1 reference

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Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcription.

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Combinatorial control of gene expression by nuclear receptors and coregulators

1 reference

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21 January 2018

Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR gamma degradation and transactivation

1 reference

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21 January 2018

The 26S proteasome: a molecular machine designed for controlled proteolysis

1 reference

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Co-regulator recruitment and the mechanism of retinoic acid receptor synergy

1 reference

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Nuclear receptors: integration of multiple signalling pathways through phosphorylation

1 reference

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The 14th Datta Lecture. TFIIH: from transcription to clinic

1 reference

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Down-regulation of the phosphatidylinositol 3-kinase/Akt pathway is involved in retinoic acid-induced phosphorylation, degradation, and transcriptional activity of retinoic acid receptor gamma 2.

1 reference

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21 January 2018

Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions

1 reference

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Involvement of all-trans-retinoic acid in the breakdown of retinoic acid receptors alpha and gamma through proteasomes in MCF-7 human breast cancer cells.

1 reference

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Promoter context- and response element-dependent specificity of the transcriptional activation and modulating functions of retinoic acid receptors

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Detection of retinoid X receptors using specific monoclonal and polyclonal antibodies.

1 reference

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Loss of retinoic acid receptor gamma function in F9 cells by gene disruption results in aberrant Hoxa-1 expression and differentiation upon retinoic acid treatment

1 reference

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21 January 2018

Phosphorylation of activation functions AF-1 and AF-2 of RARalpha and RARgamma is indispensable for differentiation of F9 cells upon retinoic acid and cAMP treatment

1 reference

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21 January 2018

Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain

1 reference

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21 January 2018

Substrate targeting in the ubiquitin system

1 reference

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Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome

1 reference

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21 January 2018

How the ubiquitin-proteasome system controls transcription

1 reference

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21 January 2018

TIF2 mediates the synergy between RARalpha 1 activation functions AF-1 and AF-2.

1 reference

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p38 mitogen-activated protein kinase activates peroxisome proliferator-activated receptor alpha: a potential role in the cardiac metabolic stress response

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From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells

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Oncogenic kinase signalling

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Her2/neu induces all-trans retinoic acid (ATRA) resistance in breast cancer cells

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TFIIH interacts with the retinoic acid receptor gamma and phosphorylates its AF-1-activating domain through cdk7

1 reference

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21 January 2018

Hyperphosphorylation of the retinoid X receptor alpha by activated c-Jun NH2-terminal kinases

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Dimerization with retinoid X receptors and phosphorylation modulate the retinoic acid-induced degradation of retinoic acid receptors alpha and gamma through the ubiquitin-proteasome pathway

1 reference

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21 January 2018

Stimulation of RARα Activation Function AF-1 through Binding to the General Transcription Factor TFIIH and Phosphorylation by CDK7

1 reference

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21 January 2018

Serine Phosphorylation-regulated Ubiquitination and Degradation of β-Catenin

1 reference

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Control of retinoic acid receptor heterodimerization by ligand-induced structural transitions. A novel mechanism of action for retinoid antagonists.

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Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1

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Identifiers

10.1074/JBC.M304952200

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

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