scholarly journals Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)

2011 ◽  
Vol 11 (4) ◽  
pp. 314-319 ◽  
Author(s):  
Jeffrey C Sivils ◽  
Cheryl L Storer ◽  
Mario D Galigniana ◽  
Marc B Cox
Keyword(s):  
Hormone Receptor ◽  
Binding Protein ◽  
Steroid Hormone ◽  
Steroid Hormone Receptor ◽  
Receptor Function ◽  
Fk506 Binding Protein

scholarly journals FK506-Binding Protein 52 Phosphorylation: A Potential Mechanism for Regulating Steroid Hormone Receptor Activity

2007 ◽  
Vol 21 (12) ◽  
pp. 2956-2967 ◽  
Author(s):  
Marc B. Cox ◽  
Daniel L. Riggs ◽  
Martin Hessling ◽  
Felix Schumacher ◽  
Johannes Buchner ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Binding Protein ◽  
Steroid Hormone ◽  
Receptor Activity ◽  
Steroid Hormone Receptor ◽  
Potential Mechanism ◽  
Fk506 Binding Protein

Levels and effect of serum pops on steroid hormone receptor function in Greenlandic Inuit

2011 ◽  
Vol 205 ◽  
pp. S296-S297
Author(s):  
T. Krüger ◽  
M. Ghisari ◽  
C. Yi ◽  
E.C. Bonefeld-Jørgensen
Keyword(s):  
Hormone Receptor ◽  
Steroid Hormone ◽  
Steroid Hormone Receptor ◽  
Receptor Function

scholarly journals Mechanism of transformation by v-ErbA: Substitution for steroid hormone receptor function in self renewal induction

Oncogene ◽  
1997 ◽  
Vol 15 (6) ◽  
pp. 701-715 ◽  
Author(s):  
Anton Bauer ◽  
Eugen Ulrich ◽  
Monika Andersson ◽  
Hartmut Beug ◽  
Marieke von Lindern
Keyword(s):  
Hormone Receptor ◽  
Steroid Hormone ◽  
Steroid Hormone Receptor ◽  
Receptor Function ◽  
Self Renewal

scholarly journals Synergistic Activation of the Prolactin Promoter by Vitamin D Receptor and GHF-1: Role of the Coactivators, CREB-Binding Protein and Steroid Hormone Receptor Coactivator-1 (SRC-1)

1999 ◽  
Vol 13 (7) ◽  
pp. 1141-1154 ◽  
Author(s):  
Ana I. Castillo ◽  
Ana M. Jimenez-Lara ◽  
Rosa M. Tolon ◽  
Ana Aranda
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Hormone Receptor ◽  
Binding Protein ◽  
Steroid Hormone ◽  
Steroid Hormone Receptor ◽  
Creb Binding Protein ◽  
Wild Type ◽  
Prl Gene

Abstract PRL gene expression is dependent on the presence of the pituitary-specific transcription factor GHF-1/Pit-1, which is transcribed in a highly restricted manner in cells of the anterior pituitary. In pituitary GH3 cells, vitamin D increases the levels of PRL transcripts and stimulates the PRL promoter. We have analyzed the role of GHF-1 and of the vitamin D receptor (VDR) to confer vitamin D responsiveness to the PRL promoter. For this purpose we have used nonpituitary HeLa cells, which do not express GHF-1. We found that VDR activates the PRL promoter both in a ligand-dependent and -independent manner through a sequence located between positions− 45/−27 in the proximal 5′-flanking region. This sequence also confers VDR and vitamin D responsiveness to a heterologous promoter. In the context of the PRL gene, VDR requires the presence of GHF-1 to activate the promoter. Truncation of the last 12 C-terminal amino acids of VDR, which contain the ligand-dependent activation function (AF2), abolishes regulation by vitamin D, suggesting that binding of coactivators to this region mediates ligand-dependent stimulation of the PRL promoter by the receptor. Indeed, expression of the coactivators, steroid hormone receptor coactivator-1 (SRC-1) and CREB-binding protein (CBP), significantly enhances the stimulatory effect of vitamin D mediated by the wild-type VDR but not by the AF2 mutant receptor. Furthermore, CBP also increases the activation of the PRL promoter by GHF-1 and the ligand-independent activation by both wild-type and mutant VDR.

scholarly journals Functional Comparison of Human and Zebra Fish FKBP52 Confirms the Importance of the Proline-Rich Loop for Regulation of Steroid Hormone Receptor Activity

2019 ◽  
Vol 20 (21) ◽  
pp. 5346 ◽  
Author(s):  
Diondra C. Harris ◽  
Yenni A. Garcia ◽  
Cheryl Storer Samaniego ◽  
Veronica W. Rowlett ◽  
Nina R. Ortiz ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Steroid Hormone ◽  
Receptor Activity ◽  
Comparative Approach ◽  
Steroid Hormone Receptor ◽  
Zebra Fish ◽  
Fk506 Binding Protein ◽  
Open Conformation ◽  
Loop Surface ◽  
Chaperone Complex

Previous studies demonstrated that the 52-kDa FK506-binding protein (FKBP52) proline-rich loop is functionally relevant in the regulation of steroid hormone receptor activity. While zebra fish (Danio rerio; Dr) FKBP52 contains all of the analogous domains and residues previously identified as critical for FKBP52 potentiation of receptor activity, it fails to potentiate activity. Thus, we used a cross-species comparative approach to assess the residues that are functionally critical for FKBP52 function. Random selection of gain-of-function DrFKBP52 mutants in Saccharomyces cerevisiae identified two critical residues, alanine 111 (A111) and threonine 157 (T157), for activation of receptor potentiation by DrFKBP52. In silico homology modeling suggests that alanine to valine substitution at position 111 in DrFKBP52 induces an open conformation of the proline-rich loop surface similar to that observed on human FKBP52, which may allow for sufficient surface area and increased hydrophobicity for interactions within the receptor–chaperone complex. A second mutation in the FKBP12-like domain 2 (FK2), threonine 157 to arginine (T157R), also enhanced potentiation, and the DrFKBP52-A111V/T157R double mutant potentiated receptor activity similar to human FKBP52. Collectively, these results confirm the functional importance of the FKBP52 proline-rich loop, suggest that an open conformation on the proline-rich loop surface is a predictor of activity, and highlight the importance of an additional residue within the FK2 domain.

scholarly journals Hsp70 Cochaperones HspBP1 and BAG-1M Differentially Regulate Steroid Hormone Receptor Function

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e85415 ◽  
Author(s):  
Regina T. Knapp ◽  
Michael J. H. Wong ◽  
Lorenz K. Kollmannsberger ◽  
Nils C. Gassen ◽  
Anja Kretzschmar ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Steroid Hormone ◽  
Steroid Hormone Receptor ◽  
Receptor Function
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