Transcriptional regulation by steroid hormones

  title={Transcriptional regulation by steroid hormones},
  author={Miguel Beato and Sebasti{\'a}n Ch{\'a}vez and Mathias Truss},

The Androgen Receptor Amino-Terminal Domain Plays a Key Role in p160 Coactivator-Stimulated Gene Transcription

The functional interactions between the androgen receptor (AR) and 160-kDa nuclear receptor coactivators are analyzed and suggest that in the native AR the efficient recruitment of coactivator requires a functional association of the NTD with the LBD and that the binding of coActivators occurs primarily through the N TD.

Glucocorticoid Receptor Structure and Function

A molecular map that integrates site-specific DNA, ligands, chromatin, coregulators and post-transcriptional modifications to determine the composition and function of gene-specific transcriptional regulatory complexes involving glucocorticoid receptor modulators is proposed.

Interaction between the Retinoid X Receptor and Transcription Factor IIB Is Ligand-dependent in Vivo *

Functional analysis and co-immunoprecipitation, far Western analysis, and glutathioneS-transferase binding studies indicate that interaction of mRXRβ with TFIIB is specific, direct, and ligand-dependent in vivo and suggest that gene activation by RXR involvesTFIIB.

Auto-silencing by the retinoid X receptor.

It is proposed that RXR acts as an auto-silencer by sequestering itself into tetramers, and that an important role for the ligand in activating this receptor is to release active species, dimers and monomers, from the transcriptionally inactive tetrameric pool.

The Classic Steroid Hormone Receptors and ERβ, the Novel Estrogen Receptor

Immunocytochemical studies with monoclonal antibodies against the various receptors indicate that most steroid hormone receptors (e.g., ER and PR) are nuclear even in the absence of hormone, although GR and MR appear to be exceptions.

Choosing the right partner in hormone-dependent gene regulation: Glucocorticoid and progesterone receptors crosstalk in breast cancer cells

The state of the art of the functional cross-talk between PR and GR in breast cancer cells is summarized and new paradigms of specificity in hormone action are discussed.

Potentiation of glucocorticoid receptor transcriptional activity by sumoylation.

A model in which SUMO-1 regulates the synergy control function of GR and serves as a unique signal for activation and destruction is proposed, largely exceeding those observed so far for other sumoylated transcription factors.

Rapid steroid hormone actions via membrane receptors.




Transcriptional control by steroid hormones: the role of chromatin.

It is implied that nucleosome positioning not only represses hormone-independent transcription, but also enables binding of a full complement of transcription factors to the hormone-responsive unit after hormone induction.

A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors.

Yeast two-hybrid system identifies a protein, thyroid hormone receptor uncoupling protein (TRUP), that specifically interacts with a region of the human thyroid hormone receptors consisting of the hinge region and the N-terminal portion of the ligand binding domain in a hormone-independent manner.

Interaction of proteins with transcriptionally active estrogen receptors.

Since the ability of these proteins to interact with the hormone binding domain correlates with its transcriptional activity, one or more of them may contribute to hormone-dependent transcriptional activation by the estrogen receptor.

Interaction of thyroid-hormone receptor with a conserved transcriptional mediator

It is shown that Tripl can functionally substitute for Sugl in yeast, and that both proteins interact in vitro with the thyroid-hormone receptor, and with the transcriptional activation domains of yeast GAL4 and of herpes virus VP16.

The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences

It is demonstrated that the high-mobility-group chromatin protein H MG-1, as a highly purified protein, dramatically enhanced binding of purified PR to PREs in gel mobility shift assays, suggesting that HMG-1 facilitates the binding of PR by inducing a structural change in the target DNA.

Identification of a Transactivation Function in the Progesterone Receptor That Interacts with the TAFII110 Subunit of the TFIID Complex (*)

In cotransfection experiments and an in vitro transcription assay, the DNA binding domain of the progesterone receptor displayed significant activation potential, suggesting that an interaction between the progestersone receptor and TAFII110 may represent an important step in the mechanism of activation.

Nuclear factor I acts as a transcription factor on the MMTV promoter but competes with steroid hormone receptors for DNA binding.

Results suggest that, though NFI acts as a transcription factor on the MMTV promoter, transcriptional activation does not take place through a direct facilitation of DNA binding of NFI by steroid hormone receptors.

Hormone induces binding of receptors and transcription factors to a rearranged nucleosome on the MMTV promoter in vivo.

Using genomic footprinting, it is shown that MMTV promoter DNA is rotationally phased in intact cells containing either episomal or chromosomally integrated proviral fragments and all relevant transcription factors bind to the surface of the rearranged nucleosome.

Estrogen regulation of proto-oncogenes coding for nuclear proteins.

Data indicating that estrogen directly activates (primary activation) expression of proto-oncogenes codifying for nuclear proteins that, in turn, are responsible for indirect activation of other genes are reviewed to envisage how estrogen can direct a complex task such as cell reproduction.