scholarly journals REV-ERBα influences stability and nuclear localization of the glucocorticoid receptor

2016 ◽  
pp. jcs.190959 ◽  
Author(s):  
Takashi Okabe ◽  
Rohit Chavan ◽  
Sara S. Fonseca Costa ◽  
Andrea Brenna ◽  
Jürgen A. Ripperger ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Nuclear Localization

Intracellular Localization of the Glucocorticoid Receptor: Evidence for Cytoplasmic and Nuclear Localization*

Endocrinology ◽  
1987 ◽  
Vol 120 (4) ◽  
pp. 1232-1242 ◽  
Author(s):  
ANN-CHARLOTTE WIKSTRÖM ◽  
ODDMUND BAKKE ◽  
SAM OKRET ◽  
MIKAEL BRÖNNEGÅRD ◽  
JAN-ÅKE GUSTAFSSON
Keyword(s):  
Glucocorticoid Receptor ◽  
Nuclear Localization ◽  
Intracellular Localization

scholarly journals Dexamethasone Modulates Nonvisual Opsins, Glucocorticoid Receptor, and Clock Genes inDanio rerioZEM-2S Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-14 ◽  
Author(s):  
Jennifer Caroline Sousa ◽  
Keila Karoline Magalhães-Marques ◽  
Sanseray da Silveira Cruz-Machado ◽  
Maria Nathalia Moraes ◽  
Ana Maria de Lauro Castrucci
Keyword(s):  
Cell Membrane ◽  
Glucocorticoid Receptor ◽  
Nuclear Localization ◽  
Clock Genes ◽  
Clock Synchronization ◽  
Cellular Distribution ◽  
Embryonic Cells ◽  
Light Conditions ◽  
Peripheral Clocks ◽  
First Time

Here we report, for the first time, the differential cellular distribution of two melanopsins (Opn4m1 and Opn4m2) and the effects of GR agonist, dexamethasone, on the expression of these opsins and clock genes, in the photosensitiveD. rerioZEM-2S embryonic cells. Immunopositive labeling for Opn4m1 was detected in the cell membrane whereas Opn4m2 labeling shows nuclear localization, which did not change in response to light.opn4m1,opn4m2,gr,per1b,andcry1bpresented an oscillatory profile of expression in LD condition. In both DD and LD condition, dexamethasone (DEX) treatment shifted the peak expression ofper1bandcry1btranscripts to ZT16, which corresponds to the highestopn4m1expression. Interestingly, DEX promoted an increase ofper1bexpression when applied in LD condition but a decrease when the cells were kept under DD condition. Although DEX effects are divergent with different light conditions, the response resulted in clock synchronization in all cases. Taken together, these data demonstrate thatD. rerioZEM-2S cells possess a photosensitive system due to melanopsin expression which results in an oscillatory profile of clock genes in response to LD cycle. Moreover, we provide evidence that glucocorticoid acts as a circadian regulator ofD. rerioperipheral clocks.

scholarly journals Discrimination between NL1- and NL2-Mediated Nuclear Localization of the Glucocorticoid Receptor

1999 ◽  
Vol 19 (2) ◽  
pp. 1025-1037 ◽  
Author(s):  
Joanne G. A. Savory ◽  
Brian Hsu ◽  
Ian R. Laquian ◽  
Ward Giffin ◽  
Terry Reich ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Nuclear Export ◽  
Binding Domain ◽  
Leptomycin B ◽  
Importin Α ◽  
Agonist And Antagonist ◽  
Import And Export ◽  
Pathway Inhibition

ABSTRACT Glucocorticoid receptor (GR) cycles between a free liganded form that is localized to the nucleus and a heat shock protein (hsp)-immunophilin-complexed, unliganded form that is usually localized to the cytoplasm but that can also be nuclear. In addition, rapid nucleocytoplasmic exchange or shuttling of the receptor underlies its localization. Nuclear import of liganded GR is mediated through a well-characterized sequence, NL1, adjacent to the receptor DNA binding domain and a second, uncharacterized motif, NL2, that overlaps with the ligand binding domain. In this study we report that rapid nuclear import (half-life [t 1/2] of 4 to 6 min) of agonist- and antagonist-treated GR and the localization of unliganded, hsp-associated GRs to the nucleus in G0 are mediated through NL1 and correlate with the binding of GR to pendulin/importin α. By contrast, NL2-mediated nuclear transfer of GR occurred more slowly (t 1/2 = 45 min to 1 h), was agonist specific, and appeared to be independent of binding to importin α. Together, these results suggest that NL2 mediates the nuclear import of GR through an alternative nuclear import pathway. Nuclear export of GR was inhibited by leptomycin B, suggesting that the transfer of GR to the cytoplasm is mediated through the CRM1-dependent pathway. Inhibition of GR nuclear export by leptomycin B enhanced the nuclear localization of both unliganded, wild-type GR and hormone-treated NL1− GR. These results highlight that the subcellular localization of both liganded and unliganded GRs is determined, at least in part, by a flexible equilibrium between the rates of nuclear import and export.

scholarly journals Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors.

1990 ◽  
Vol 1 (3) ◽  
pp. 291-299 ◽  
Author(s):  
D Picard ◽  
V Kumar ◽  
P Chambon ◽  
K R Yamamoto
Keyword(s):  
Signal Transduction ◽  
Estrogen Receptor ◽  
Glucocorticoid Receptor ◽  
Nuclear Localization ◽  
Glucocorticoid Receptors ◽  
Common Mechanism ◽  
Hormone Binding ◽  
Nuclear Localization Signals ◽  
Binding Regions ◽  
Human Estrogen Receptor

The glucocorticoid receptor accumulates in nuclei only in the presence of bound hormone, whereas the estrogen receptor has been reported to be constitutively nuclear. To investigate this distinction, we compared the nuclear localization domains of the two receptors and the capacity of their respective hormone-binding regions to regulate nuclear localization activity. As with the glucocorticoid receptor, we showed that the human estrogen receptor contained a nuclear localization signal between the DNA-binding and hormone-binding regions (amino acids 256-303); however, in contrast to the glucocorticoid receptor, the estrogen receptor lacked a second nuclear localization domain within the hormone-binding region. Moreover, the hormone-binding domain of the unliganded estrogen receptor failed to regulate nuclear localization signals, although it efficiently regulated other receptor functions. We conclude that the two receptors employ a common mechanism for signal transduction involving a novel "inactivation" function, but that they differ in their control of nuclear localization. Thus, despite the strong relatedness of the estrogen and glucocorticoid receptors in structure and activity, certain differences in their properties could have important functional implications.

scholarly journals The HIV-1 Vpr and glucocorticoid receptor complex is a gain-of-function interaction that prevents the nuclear localization of PARP-1

2006 ◽  
Vol 8 (2) ◽  
pp. 170-179 ◽  
Author(s):  
Karuppiah Muthumani ◽  
Andrew Y. Choo ◽  
Wei-Xing Zong ◽  
Muniswamy Madesh ◽  
Daniel S. Hwang ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Nuclear Localization ◽  
Receptor Complex ◽  
Gain Of Function ◽  
Parp 1 ◽  
Hiv 1
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