Structure and function of the dioxin receptor: A DNA-binding protein similar to steroid hormone receptors

Chemosphere ◽  
1987 ◽  
Vol 16 (8-9) ◽  
pp. 1681-1686
Author(s):  
Lorenz Poellinger ◽  
Anna Wilhelmsson ◽  
Scott Cuthill ◽  
Johan Lund ◽  
Peter Söderkvist ◽  
...  
Keyword(s):  
Dna Binding ◽  
Hormone Receptors ◽  
Binding Protein ◽  
Steroid Hormone ◽  
Dna Binding Protein ◽  
Structure And Function ◽  
Steroid Hormone Receptors ◽  
And Function ◽  
Dioxin Receptor

Steroid hormone receptors: Cloning, structure and function

1986 ◽  
Vol 25 ◽  
pp. 97
Author(s):  
S. Green ◽  
P. Walter ◽  
V. Kumar ◽  
A. Krust ◽  
P. Argos ◽  
...  
Keyword(s):  
Hormone Receptors ◽  
Steroid Hormone ◽  
Structure And Function ◽  
Steroid Hormone Receptors ◽  
And Function

scholarly journals Structure and function of phage p2 ORF34p2, a new type of single-stranded DNA binding protein

2009 ◽  
Vol 73 (6) ◽  
pp. 1156-1170 ◽  
Author(s):  
Erika Scaltriti ◽  
Mariella Tegoni ◽  
Claudio Rivetti ◽  
Hélène Launay ◽  
Jean-Yves Masson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Structure And Function ◽  
Single Stranded Dna ◽  
New Type ◽  
And Function

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 Study of the structure and function of the HURP protein during mitotic division

2013 ◽  
Author(s):  
Κωνσταντίνος Νάκος
Keyword(s):  
Dna Binding ◽  
Xenopus Laevis ◽  
Histone Deacetylase ◽  
Dna Binding Protein ◽  
Mitotic Division ◽  
Structure And Function ◽  
Aurora A ◽  
Nucleosome Remodeling ◽  
And Function

Η πρωτεΐνη HURP (Hepatoma Up-Regulated protein) έχει αναγνωριστεί ως παράγονταςσυναρμολόγησης της ατράκτου (SAF) που ρυθμίζεται από τη RanGTP. Αρχικά βρέθηκε σε μιτωτικάεκχυλίσματα αυγών Xenopus laevis, σε σύμπλοκο με τις TPX2, XMAP215, Eg5 και Aurora A. Η HURPπροσδένεται στους μικροσωληνίσκους, εντοπίζεται κυρίως στους μικροσωληνίσκους των κινητοχώρωνκαι είναι απαραίτητη για την σωστή συναρμολόγηση της μιτωτικής ατράκτου. Παρόλο αυτά, πρωτεΐνεςπου αλληλεπιδρούν με τη HURP σε ανθρώπινα κύτταρα παραμένουν άγνωστες.Σε αυτή τη μελέτη περιγράφουμε την αναγνώριση μίας νέας πρωτεΐνης που αλληλεπιδρά με τη HURP,τη CHD4 (Chromodomain Helicase DNA binding protein 4) μία ATPάση της αναδιαμόρφωσης τηςχρωματίνης και καταλυτική υπομονάδα του συμπλόκου αποκετυλασών που ευθύνεται για τηναναδιαμόρφωση του νουκλεοσώματος (Nucleosome remodeling and histone Deacetylase - NuRD).Πρόσφατα η πρωτεΐνη CHD4 αναγνωρίστηκε ως πρωτεΐνη που προσδένεται στους μικροσωληνίσκουςκαι ρυθμίζεται από την RanGTP.Οι μελέτες μας σε ανθρώπινα κύτταρα έδειξαν ότι η CHD4 κατά τη μίτωση απελευθερώνεται από ταμιτωτικά χρωμοσώματα και εντοπίζεται στην άτρακτο, υποδεικνύοντας ένα καινούριο ρόλο της CHD4στη συναρμολόγηση της ατράκτου. Για να κατανοήσουμε τη λειτουργία της CHD4 πραγματοποιήσαμεμελέτες απαλοιφής της CHD4 με την τεχνική της αποσιώπισης γονιδίου με siRNA. Μείωση της CHD4προκαλεί βλάβες στη συναρμολόγηση της μιτωτικής ατράκτου και στη στοίχιση των χρωμοσωμάτωνστις αρχές της μίτωσης, οδηγώντας σε ανώμαλο διαχωρισμό των χρωμοσωμάτων. Επιπλέον, ηαπώλεια της CHD4 επηρρεάζει τη σταθερότητα των K-fibers μειώνοντας σημαντικά την ποσότητα των μικροσωληνίσκων των κινητοχώρων. Μετά την απαλοιφή της CHD4, ο εντοπισμός της HURP βρέθηκενα αλλάζει, χάνοντας την προτίμησή της για τους μικροσωληνίσκους, των κινητοχώρων,υποδεικνύοντας την πιθανή ρύθμιση του εντοπισμού της HURP από την CHD4. Τέλος από in vitro καιin vivo πειράματα, βρήκαμε ότι η CHD4 αλληλεπιδρά με τη μιτωτική κινάση Aurora A και την πρωτεΐνηTPX2 που συνδέεται με μικροσωληνίσκους, δημιουργώντας ένα καινούριο σύμπλοκο σημαντικό για τηλειτουργία της μιτωτικής ατράκτου στα κύτταρα θηλαστικών.

scholarly journals Hsp90 Heterocomplexes Regulate Steroid Hormone Receptors: From Stress Response to Psychiatric Disease

2018 ◽  
Vol 20 (1) ◽  
pp. 79 ◽  
Author(s):  
Jeremy Baker ◽  
Ilayda Ozsan ◽  
Santiago Rodriguez Ospina ◽  
Danielle Gulick ◽  
Laura Blair
Keyword(s):  
Stress Response ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Steroid Receptor ◽  
Steroid Hormone Receptors ◽  
Psychiatric Disease ◽  
Post Traumatic Stress ◽  
Fk506 Binding Protein ◽  
Structural Regulation ◽  
And Function

The hypothalamus-pituitary-adrenal (HPA) axis directly controls the stress response. Dysregulation of this neuroendocrine system is a common feature among psychiatric disorders. Steroid hormone receptors, like glucocorticoid receptor (GR), function as transcription factors of a diverse set of genes upon activation. This activity is regulated by molecular chaperone heterocomplexes. Much is known about the structure and function of these GR/heterocomplexes. There is strong evidence suggesting altered regulation of steroid receptor hormones by chaperones, particularly the 51 kDa FK506-binding protein (FKBP51), may work with environmental factors to increase susceptibility to various psychiatric illnesses including post-traumatic stress disorder (PTSD), major depressive disorder (MDD), and anxiety. This review highlights the regulation of steroid receptor dynamics by the 90kDa heat shock protein (Hsp90)/cochaperone heterocomplexes with an in depth look at how the structural regulation and imbalances in cochaperones can cause functional effects on GR activity. Links between the stress response and circadian systems and the development of novel chaperone-targeting therapeutics are also discussed.

Antiandrogens as environmental endocrine disruptors¤

1998 ◽  
Vol 10 (1) ◽  
pp. 105 ◽  
Author(s):  
W. R. Kelce ◽  
L. E. Gray ◽  
E. M. Wilson
Keyword(s):  
Androgen Receptor ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Sex Differentiation ◽  
Environmental Chemicals ◽  
Steroid Hormone Receptors ◽  
Environmental Endocrine Disruptors ◽  
And Function

Steroid hormone receptors control fundamental events in embryonic development and sex differentiation through their function as ligand-inducible transcription factors. The consequences of disrupting these processes can be especially profound during development due to the crucial role hormones play in controlling transient and irreversible developmental processes. Several environmental chemicals, including metabolites of the fungicide vinclozolin and the pesticide DDT, disrupt male reproductive development and function by inhibiting androgen receptor mediated events. A variety of in vitro and in vivo approaches have been used to determine the molecular basis of environmental antiandrogen toxicity. These chemicals commonly bind androgen receptor with moderate affinity and act as antagonists by inhibiting transcription of androgen dependent genes.

Sign in / Sign up

Export Citation Format

Share Document