Subcellular localization and mechanisms of nucleocytoplasmic trafficking of steroid receptor coactivator-1. (Q40641807)

22 September 2017

Subcellular localization and mechanisms of nucleocytoplasmic trafficking of steroid receptor coactivator-1. (English)

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22 September 2017

Jacques Pantel

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Anne Chauchereau

object named as

Anne Chauchereau

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author name string

Larbi Amazit

1

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22 September 2017

Youssef Alj

2

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22 September 2017

Rakesh Kumar Tyagi

3

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22 September 2017

Hugues Loosfelt

5

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22 September 2017

Christophe Pichon

6

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22 September 2017

Emmanuelle Foulon-Guinchard

8

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22 September 2017

Philippe Leclerc

9

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22 September 2017

Edwin Milgrom

10

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22 September 2017

Anne Guiochon-Mantel

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22 September 2017

language of work or name

English

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publication date

4 June 2003

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Journal of Biological Chemistry

22 September 2017

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22 September 2017

278

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22 September 2017

34

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22 September 2017

32195-32203

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The steroid and thyroid hormone receptor superfamily

22 September 2017

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Trafficking of nuclear receptors in living cells

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The Ernst Schering Poster Award. Intracellular traffic of steroid hormone receptors

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Regulation of steroid receptor subcellular trafficking

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Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers

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Acetylation of histones and transcription-related factors

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Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions.

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Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription

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Coactivator and corepressor complexes in nuclear receptor function

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Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase

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Regulation of somatic growth by the p160 coactivator p/CIP

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Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300

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TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1

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The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function

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A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors

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A splicing variant of Steroid Receptor Coactivator-1 (SRC-1E): the major isoform of SRC-1 to mediate thyroid hormone action

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Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor

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JAB1 interacts with both the progesterone receptor and SRC-1

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Effect of PML and PML-RAR on the transactivation properties and subcellular distribution of steroid hormone receptors

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Mechanisms of progesterone receptor export from nuclei: role of nuclear localization signal, nuclear export signal, and ran guanosine triphosphate

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Two-subunit structure of the human thyrotropin receptor

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Nuclear localization signals also mediate the outward movement of proteins from the nucleus

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Dynamics of estrogen receptor turnover in uterine cells in vitro and in uteri in vivo

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Monoclonal antibody specific for human nuclear proteins IEF 8Z30 and 8Z31 accumulates in the nucleus a few hours after cytoplasmic microinjection of cells expressing these proteins

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The nuclear hormone receptor coactivator SRC-1 is a specific target of p300.

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Differential effects of nuclear receptor corepressor (N-CoR) expression levels on retinoic acid receptor-mediated repression support the existence of dynamically regulated corepressor complexes

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Constitutive activation of the aromatic hydrocarbon receptor

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Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1

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Histone deacetylase 4 possesses intrinsic nuclear import and export signals

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Aryl hydrocarbon receptor imported into the nucleus following ligand binding is rapidly degraded via the cytosplasmic proteasome following nuclear export

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CRM1-mediated recycling of snurportin 1 to the cytoplasm

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Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4.

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Regulation of nuclear localization: a key to a door

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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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Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits

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Microtubule-dependent subcellular redistribution of the transcriptional coactivator p/CIP.

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21 January 2018

Identifiers

DOI

10.1074/JBC.M300730200

1 reference

22 September 2017

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