HSP90 chaperone cycle for steroid hormone receptors (SHR)

2017 ◽  
Vol 60 ◽  
Author(s):  
D Picard ◽  
PC Echeverria
Keyword(s):  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors ◽  
Hsp90 Chaperone

STEROID HORMONE RECEPTORS AND CLINICAL RELEVANCE

1975 ◽  
Vol 80 (1_Suppla) ◽  
pp. S160-S161 ◽  
Author(s):  
H. Maass
Keyword(s):  
Clinical Relevance ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors

The Bovine Cervix During the Oestrous Cycle: Regional Differences in Morphology and Density of Steroid Hormone Receptors

2000 ◽  
Vol 35 (3-4) ◽  
pp. 120-124 ◽  
Author(s):  
VNA Breeveld-Dwarkasing ◽  
GC van der Weijden ◽  
MAM Taverne ◽  
FMF van Dissel-Emiliani
Keyword(s):  
Regional Differences ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Oestrous Cycle ◽  
Steroid Hormone Receptors

877 ROLE OF STEROID HORMONE RECEPTORS ON FORMATION AND PROGRESSION OF BLADDER CARCINOMA

2011 ◽  
Vol 185 (4S) ◽  
Author(s):  
Gholamreza Pourmand ◽  
Sepehr Salem ◽  
Abdolrasoul Mehrsai ◽  
Farid Kosari
Keyword(s):  
Bladder Carcinoma ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors

Steroid Hormone Receptors and Human Breast Cancer

1985 ◽  
Vol 16 (5) ◽  
pp. 287-294 ◽  
Author(s):  
Dawn M. Mirecki ◽  
V. Craig Jordan
Keyword(s):  
Breast Cancer ◽  
Human Breast Cancer ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors ◽  
Human Breast

The steroid hormone receptors in tumors of adipose tissue

1985 ◽  
Vol 28 (2) ◽  
pp. 87-89 ◽  
Author(s):  
P. K. Chaudhuri ◽  
M. J. Walker ◽  
C. W. Beattie ◽  
T. K. Das Gupta
Keyword(s):  
Adipose Tissue ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Hormone Receptors

Comparative analysis of the influence of the high-mobility group box 1 protein on DNA binding and transcriptional activation by the androgen, glucocorticoid, progesterone and mineralocorticoid receptors

2001 ◽  
Vol 361 (1) ◽  
pp. 97-103 ◽  
Author(s):  
Guy VERRIJDT ◽  
Annemie HAELENS ◽  
Erik SCHOENMAKERS ◽  
Wilfried ROMBAUTS ◽  
Frank CLAESSENS
Keyword(s):  
Androgen Receptor ◽  
Comparative Analysis ◽  
Dna Binding ◽  
Mineralocorticoid Receptor ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
High Mobility ◽  
Steroid Hormone Receptors ◽  
High Mobility Group ◽  
Mineralocorticoid Receptors

We performed a comparative analysis of the effect of high-mobility group box protein 1 (HMGB1) on DNA binding by the DNA-binding domains (DBDs) of the androgen, glucocorticoid, progesterone and mineralocorticoid receptors. The affinity of the DBDs of the different receptors for the tyrosine aminotransferase glucocorticoid response element, a classical high-affinity binding element, was augmented up to 7-fold by HMGB1. We found no major differences in the effects of HMGB1 on DNA binding between the different steroid hormone receptors. In transient transfection assays, however, HMGB1 significantly enhances the activity of the glucocorticoid and progesterone receptors but not the androgen or mineralocorticoid receptor. We also investigated the effect of HMGB1 on the binding of the androgen receptor DBD to a subclass of directly repeated response elements that is recognized exclusively by the androgen receptor and not by the glucocorticoid, progesterone or mineralocorticoid receptor. Surprisingly, a deletion of 26 amino acid residues from the C-terminal extension of the androgen receptor DBD does not influence DNA binding but destroys its sensitivity to HMGB1. Deletion of the corresponding fragment in the DBDs of the glucocorticoid, progesterone and mineralocorticoid receptor destroyed their DNA binding. This 26-residue fragment is therefore essential for the influence of HMGB1 on DNA recognition by all steroid hormone receptors that were tested. However, it is dispensable for DNA binding by the androgen receptor.

scholarly journals E6-associated protein (E6-AP) is a dual function coactivator of steroid hormone receptors

2008 ◽  
Vol 6 (1) ◽  
pp. nrs.06006 ◽  
Author(s):  
Sivapriya Ramamoorthy ◽  
Zafar Nawaz
Keyword(s):  
Hormone Receptors ◽  
Target Genes ◽  
Steroid Hormone ◽  
Enzymatic Activities ◽  
Steroid Hormone Receptors ◽  
Dual Function ◽  
Biological Functions ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Steroid hormone receptors (SHR) belong to a large family of ligand-activated transcription factors that perform their biological functions by enhancing the transcription of specific target genes. The transactivation functions of SHRs are regulated by a specialized group of proteins called coactivators. The SHR coactivators represent a growing class of proteins with various enzymatic activities that serve to modify the chromatin to facilitate the transcription of SHR target genes. The ubiquitin-proteasome pathway enzymes have also been added to the growing list of enzymatic activities that are recruited to the SHR target gene promoters during transcription. One such ubiquitin-proteasome pathway enzyme to be identified and characterized as a SHR coactivator was E6-associated protein (E6-AP). E6-AP is a hect (homologous to E6-associated protein carboxy-terminal domain) domain containing E3 ubiquitin ligase that possesses two independent separable functions; a coactivation function and an ubiquitin-protein ligase activity. Being a component of the ubiquitin-proteasome pathway, it is postulated that E6-AP may orchestrate the dynamics of steroid hormone receptor-mediated transcription by regulating the degradation of the transcriptional complexes. E6-AP has also been shown to be involved in the regulation of various aspects of reproduction such as prostate and mammary gland development. Furthermore, it has been demonstrated that E6-AP expression is down-regulated in breast and prostate tumors and that the expression of E6-AP is inversely associated with that of estrogen and androgen receptors. This review summarizes our current knowledge about the structures, molecular mechanisms, spatiotemporal expression patterns and biological functions of E6-AP.

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