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 Phosphorylation on Tyrosine ofin VitroSynthesized Human Estrogen Receptor Activates Its Hormone Binding

1989 ◽  
Vol 3 (7) ◽  
pp. 1061-1069 ◽  
Author(s):  
A. Migliaccio ◽  
M. Di Domenico ◽  
S. Green ◽  
A. de Falco ◽  
E. L. Kajtaniak ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Hormone Binding ◽  
Human Estrogen Receptor

scholarly journals Identification of Amino Acids in the Hormone Binding Domain of the Human Estrogen Receptor Important in Estrogen Binding

1996 ◽  
Vol 271 (33) ◽  
pp. 20053-20059 ◽  
Author(s):  
Kirk Ekena ◽  
Karen E. Weis ◽  
John A. Katzenellenbogen ◽  
Benita S. Katzenellenbogen
Keyword(s):  
Amino Acids ◽  
Estrogen Receptor ◽  
Binding Domain ◽  
Hormone Binding ◽  
Human Estrogen Receptor ◽  
Estrogen Binding ◽  
Hormone Binding Domain

Different regions of the estrogen receptor are required for synergistic action with the glucocorticoid and progesterone receptors

1989 ◽  
Vol 9 (12) ◽  
pp. 5324-5330
Author(s):  
A C Cato ◽  
H Ponta
Keyword(s):  
Estrogen Receptor ◽  
Glucocorticoid Receptor ◽  
Binding Sites ◽  
Glucocorticoid Receptors ◽  
Steroid Receptors ◽  
Gene Activation ◽  
Synergistic Action ◽  
Receptor Expression ◽  
Expression Vectors ◽  
Mutant Receptor

Estrogen and progesterone or estrogen and glucocorticoid receptors functionally cooperate in gene activation if their cognate binding sites are close to one another. These interactions have been described as synergism of action of the steroid receptors. The mechanism by which synergism is achieved is not clear, although protein-protein interaction of the receptors is one of the favorite models. In transfection experiments with receptor expression vectors and a reporter gene containing estrogen and progesterone-glucocorticoid receptor binding sites, we have examined the effects that different portions of the various receptors have on synergism. N-terminal domains of the chicken progesterone and human glucocorticoid receptors, when deleted, abolished the synergistic action of these receptors with the estrogen receptor. Deletion of the carboxy-terminal amino acids 341 to 595 of the estrogen receptor produced a mutant receptor that could not trans-activate on its own. This mutant receptor did not affect the action of the glucocorticoid receptor but functioned synergistically with the progesterone receptor. We therefore conclude that the synergistic action of the receptors for estrogen and progesterone is mechanistically different from the synergistic action of the receptors for estrogen and glucocorticoid.

scholarly journals Different regions of the estrogen receptor are required for synergistic action with the glucocorticoid and progesterone receptors.

1989 ◽  
Vol 9 (12) ◽  
pp. 5324-5330 ◽  
Author(s):  
A C Cato ◽  
H Ponta
Keyword(s):  
Estrogen Receptor ◽  
Glucocorticoid Receptor ◽  
Binding Sites ◽  
Glucocorticoid Receptors ◽  
Steroid Receptors ◽  
Gene Activation ◽  
Synergistic Action ◽  
Receptor Expression ◽  
Expression Vectors ◽  
Mutant Receptor

Estrogen and progesterone or estrogen and glucocorticoid receptors functionally cooperate in gene activation if their cognate binding sites are close to one another. These interactions have been described as synergism of action of the steroid receptors. The mechanism by which synergism is achieved is not clear, although protein-protein interaction of the receptors is one of the favorite models. In transfection experiments with receptor expression vectors and a reporter gene containing estrogen and progesterone-glucocorticoid receptor binding sites, we have examined the effects that different portions of the various receptors have on synergism. N-terminal domains of the chicken progesterone and human glucocorticoid receptors, when deleted, abolished the synergistic action of these receptors with the estrogen receptor. Deletion of the carboxy-terminal amino acids 341 to 595 of the estrogen receptor produced a mutant receptor that could not trans-activate on its own. This mutant receptor did not affect the action of the glucocorticoid receptor but functioned synergistically with the progesterone receptor. We therefore conclude that the synergistic action of the receptors for estrogen and progesterone is mechanistically different from the synergistic action of the receptors for estrogen and glucocorticoid.

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