(Q24296721)

English

Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARgamma) and represses RARgamma-mediated transcription

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scholarly article

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Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARgamma) and represses RARgamma-mediated transcription (English)

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phosphorylation

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Sorbin and SH3 domain containing 3

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GOA release 2020-03-11

Retinoic acid receptor, gamma

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GOA release 2020-03-11

author name string

Gaétan Bour

1

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Jean-Luc Plassat

2

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Annie Bauer

3

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Sébastien Lalevée

4

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Cécile Rochette-Egly

5

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language of work or name

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publication date

29 April 2005

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Journal of Biological Chemistry

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280

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17027-37

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17

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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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Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently

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Nuclear retinoid receptors and the transcription of retinoid-target genes

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Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7

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Combinatorial control of gene expression by nuclear receptors and coregulators

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XPD mutations prevent TFIIH-dependent transactivation by nuclear receptors and phosphorylation of RARalpha

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A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors

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Phosphoserine/threonine-binding domains

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The nuclear receptor corepressor (N-CoR) modulates basal and activated transcription of genes controlled by retinoic acid

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Nuclear receptors in cell life and death.

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Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases

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

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The sorbin homology domain: a motif for the targeting of proteins to lipid rafts

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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

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Reexpression of retinoic acid receptor (RAR) gamma or overexpression of RAR alpha or RAR beta in RAR gamma-null F9 cells reveals a partial functional redundancy between the three RAR types

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Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities.

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

1 reference

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Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor.

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

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SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor

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The focal adhesion protein vinexin alpha regulates the phosphorylation and activity of estrogen receptor alpha

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Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin

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Retinoic acid receptor gamma: specific immunodetection and phosphorylation

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Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization

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

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

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Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha

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Minireview: nuclear receptor coactivators--an update

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Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions

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Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity.

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Identifiers

10.1074/JBC.M501344200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

release_wyktrpughvfodg37hsrmyvwkue

1 reference

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24 November 2022

based on heuristic

mapped directly with Wikidata item

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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