scholarly journals Glucocorticoid receptor dimerization induces MKP1 to protect against TNF-induced inflammation

2012 ◽  
Vol 122 (12) ◽  
pp. 4748-4748
Author(s):  
Sofie Vandevyver ◽  
Lien Dejager ◽  
Tom Van Bogaert ◽  
Anna Kleyman ◽  
Yusen Liu ◽  
...  
PLoS ONE ◽  
2019 ◽  
Vol 14 (12) ◽  
pp. e0226753
Author(s):  
Kelly Van Looveren ◽  
Michiel Van Boxelaere ◽  
Zsuzsanna Callaerts-Vegh ◽  
Claude Libert

Cell ◽  
2002 ◽  
Vol 110 (1) ◽  
pp. 93-105 ◽  
Author(s):  
Randy K. Bledsoe ◽  
Valerie G. Montana ◽  
Thomas B. Stanley ◽  
Chris J. Delves ◽  
Christopher J. Apolito ◽  
...  

2012 ◽  
Vol 18 (9) ◽  
pp. 1006-1017 ◽  
Author(s):  
M N Silverman ◽  
P Mukhopadhyay ◽  
E Belyavskaya ◽  
L H Tonelli ◽  
B D Revenis ◽  
...  

2021 ◽  
Vol 5 (Supplement_1) ◽  
pp. A809-A809
Author(s):  
Filipp Frank ◽  
Xu Liu ◽  
Eric Ortlund

Abstract The glucocorticoid receptor (GR) is a ligand-regulated transcription factor (TF) that controls the tissue- and gene-specific transactivation and transrepression of thousands of target genes. Distinct GR DNA binding sequences with activating or repressive activities have been identified, but how they modulate transcription in opposite ways is not known. We show that GR forms phase-separated condensates that specifically concentrate known co-regulators via their intrinsically disordered regions (IDRs) in vitro. A combination of dynamic, multivalent (between IDRs) and specific, stable interactions (between LxxLL motifs and the GR ligand binding domain) control the degree of recruitment. Importantly, GR DNA-binding directs the selective partitioning of co-regulators within GR condensates such that activating DNAs cause enhanced recruitment of co-activators. Our work shows that condensation controls GR function by modulating co-regulator recruitment and provides a mechanism for the up- and down-regulation of GR target genes controlled by distinct DNA recognition elements.


2017 ◽  
Vol 13 (7S_Part_6) ◽  
pp. P308-P309
Author(s):  
Carla M. Yuede ◽  
Clare E. Wallace ◽  
Hannah M. Edwards ◽  
Kayla M. Yuede ◽  
Todd A. Davis ◽  
...  

2009 ◽  
Vol 285 (11) ◽  
pp. 8061-8075 ◽  
Author(s):  
Steven Robertson ◽  
Fatima Allie-Reid ◽  
Wim Vanden Berghe ◽  
Koch Visser ◽  
Anke Binder ◽  
...  

2020 ◽  
Vol 10 ◽  
Author(s):  
Martin Wepler ◽  
Jonathan M. Preuss ◽  
Tamara Merz ◽  
Clair Hartmann ◽  
Ulrich Wachter ◽  
...  

2021 ◽  
Vol 118 (30) ◽  
pp. e2024685118
Author(s):  
Filipp Frank ◽  
Xu Liu ◽  
Eric A. Ortlund

The glucocorticoid receptor (GR) is a ligand-regulated transcription factor (TF) that controls the tissue- and gene-specific transactivation and transrepression of thousands of target genes. Distinct GR DNA-binding sequences with activating or repressive activities have been identified, but how they modulate transcription in opposite ways is not known. We show that GR forms phase-separated condensates that specifically concentrate known coregulators via their intrinsically disordered regions (IDRs) in vitro. A combination of dynamic, multivalent (between IDRs) and specific, stable interactions (between LxxLL motifs and the GR ligand-binding domain) control the degree of recruitment. Importantly, GR DNA binding directs the selective partitioning of coregulators within GR condensates such that activating DNAs cause enhanced recruitment of coactivators. Our work shows that condensation controls GR function by modulating coregulator recruitment and provides a mechanism for the up- and down-regulation of GR target genes controlled by distinct DNA recognition elements.


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