Targets of activated steroid hormone receptors: basal transcription factors and receptor interacting proteins

1998 ◽  
Vol 76 (7) ◽  
pp. 490-496 ◽  
Author(s):  
L. Klein-Hitpass ◽  
C. Schwerk ◽  
S. Kahmann ◽  
L. Vaßen
Keyword(s):  
Transcription Factors ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors ◽  
Interacting Proteins ◽  
Basal Transcription ◽  
Basal Transcription Factors ◽  
Receptor Interacting Proteins

Interaction of steroid hormone receptors with transcription factors involves chromatin remodelling

1996 ◽  
Vol 56 (1-6) ◽  
pp. 47-59 ◽  
Author(s):  
Miguel Beato ◽  
Reyes Candau ◽  
Sebastián Chávez ◽  
Christian Möws ◽  
Mathias Truss
Keyword(s):  
Transcription Factors ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Chromatin Remodelling ◽  
Steroid Hormone Receptors

Clustered Arrangement and Interaction of Steroid Hormone Receptors with Other Transcription Factors

1989 ◽  
pp. 21-28 ◽  
Author(s):  
R. Renkawitz ◽  
R. Schüle ◽  
C. Kaltschmidt ◽  
C. Baniahmad ◽  
A. Baniahmad ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors

scholarly journals Chaperoning steroid hormone signaling via reversible acetylation

2005 ◽  
Vol 3 (1) ◽  
pp. nrs.03004 ◽  
Author(s):  
Jeffrey J. Kovacs ◽  
Todd J. Cohen ◽  
Tso-Pang Yao
Keyword(s):  
Transcription Factors ◽  
Molecular Chaperone ◽  
Hormone Receptors ◽  
Binding Capacity ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors ◽  
Hormone Signaling ◽  
Protein Acetylation ◽  
Steroid Hormone Signaling ◽  
Chaperone Complex

Glucocorticoid receptor (GR) and related steroid hormone receptors are ligand-dependent transcription factors whose regulation is critical for both homeostasis and diseases. The structural maturation of the GR has been shown to require the Hsp90 molecular chaperone complex. Evidence indicates that Hsp90-dependent maturation is critical for GR ligand binding capacity and activity. While the role for Hsp90 in GR function is well established, the regulation of this process is not well understood. Here we discuss a recent finding that identifies reversible protein acetylation controlled by the deacetylase HDAC6 as a novel mechanism that regulates Hsp90-dependent GR maturation. We will also speculate on the implications of this finding in steroid hormone signaling, oncogenic transformation and its potential therapeutic utility.

scholarly journals Allosteric Modulators of Steroid Hormone Receptors: Structural Dynamics and Gene Regulation

2012 ◽  
Vol 33 (2) ◽  
pp. 271-299 ◽  
Author(s):  
Raj Kumar ◽  
Iain J. McEwan
Keyword(s):  
Transcription Factors ◽  
Hormone Receptors ◽  
Steroid Receptors ◽  
Steroid Hormone ◽  
Allosteric Regulation ◽  
Steroid Hormone Receptors ◽  
Receptor Proteins ◽  
Intrinsically Disordered ◽  
Terminal Domain ◽  
And Function

Steroid hormones are synthesized from cholesterol primarily in the adrenal gland and the gonads and play vital roles in normal physiology, the control of development, differentiation, metabolic homeostasis, and reproduction. The actions of these small lipophilic molecules are mediated by intracellular receptor proteins. It is just over 25 yr since the first cDNA for steroid receptors were cloned, a development that led to the birth of a superfamily of ligand-activated transcription factors: the nuclear receptors. The receptor proteins share structurally and functionally related ligand binding and DNA-binding domains but possess distinct N-terminal domains and hinge regions that are intrinsically disordered. Since the original cloning experiments, considerable progress has been made in our understanding of the structure, mechanisms of action, and biology of this important class of ligand-activated transcription factors. In recent years, there has been interest in the structural plasticity and function of the N-terminal domain of steroid hormone receptors and in the allosteric regulation of protein folding and function in response to hormone, DNA response element architecture, and coregulatory protein binding partners. The N-terminal domain can exist as an ensemble of conformers, having more or less structure, which prime this region of the receptor to rapidly respond to changes in the intracellular environment through hormone binding and posttranslation modifications. In this review, we address the question of receptor structure and function dynamics with particular emphasis on the structurally flexible N-terminal domain, intra- and interdomain communications, and the allosteric regulation of receptor action.

scholarly journals Signalling mechanisms in progesterone-neurotransmitter interactions

2003 ◽  
Vol 30 (2) ◽  
pp. 127-137 ◽  
Author(s):  
S Mani
Keyword(s):  
Signal Transduction ◽  
Sexual Behavior ◽  
Transcription Factors ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Transcriptional Response ◽  
Steroid Hormone Receptors ◽  
Signal Transduction Pathways ◽  
Hormone Action ◽  
Signaling Mechanisms

The current and expanded view of transcriptional regulation by the steroid/thyroid superfamily of nuclear transcription factors integrates not only the hormone-dependent but also the hormone-independent cellular signaling mechanisms in physiology and reproduction. This effort has vastly been aided by the identification of steroid hormone receptors as transcriptional mediators of a variety of ligands, whose transcriptional response is dependent upon cross-talk with distinct signal transduction pathways, their recruitment of coregulators, alteration of chromatin structure and identification of specific interactive motifs within the receptors themselves. This review will provide a framework for the current concepts in the field of steroid hormone action as exemplified by our studies on progesterone receptor in female sexual behavior.

scholarly journals The emerging role of Krüppel-like factors in endocrine-responsive cancers of female reproductive tissues

2009 ◽  
Vol 204 (3) ◽  
pp. 223-231 ◽  
Author(s):  
R C M Simmen ◽  
J M P Pabona ◽  
M C Velarde ◽  
C Simmons ◽  
O Rahal ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Hormone Receptors ◽  
Cancer Survival ◽  
Steroid Hormone ◽  
Gene Promoter ◽  
Steroid Hormone Receptors ◽  
Transcriptional Networks ◽  
Breast Cancers ◽  
Preferential Binding ◽  
Carboxy Terminal

Krüppel-like factors (KLFs), of which there are currently 17 known protein members, belong to the specificity protein (Sp) family of transcription factors and are characterized by the presence of Cys2/His2 zinc finger motifs in their carboxy-terminal domains that confer preferential binding to GC/GT-rich sequences in gene promoter and enhancer regions. While previously regarded to simply function as silencers of Sp1 transactivity, many KLFs are now shown to be relevant to human cancers by their newly identified abilities to mediate crosstalk with signaling pathways involved in the control of cell proliferation, apoptosis, migration, and differentiation. Several KLFs act as tumor suppressors and/or oncogenes under distinct cellular contexts, underscoring their prognostic potential for cancer survival and outcome. Recent studies suggest that a number of KLFs can influence steroid hormone signaling through transcriptional networks involving steroid hormone receptors and members of the nuclear receptor family of transcription factors. Since inappropriate sensitivity or resistance to steroid hormone actions underlies endocrine-related malignancies, we consider the intriguing possibility that dysregulation of expression and/or activity of KLF members is linked to the pathogenesis of endometrial and breast cancers. In this review, we focus on recently described mechanisms of actions of several KLFs (KLF4, KLF5, KLF6, and KLF9) in cancers of the mammary gland and uterus. We suggest that understanding the mode of actions of KLFs and their functional networks may lead to the development of novel therapeutics to improve current prospects for cancer prevention and cure.

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