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Kinases and protein phosphorylation as regulators of steroid hormone action
Although the primary signal for the activation of steroid hormone receptors is binding of hormone, there is increasing evidence that the activities of cell signaling pathways and the phosphorylation status of these transcription factors and their coregulators determine the overall response to the ho...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Nuclear Receptor Signaling Atlas
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1876600/ https://www.ncbi.nlm.nih.gov/pubmed/17525795 http://dx.doi.org/10.1621/nrs.05005 |
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author | Weigel, Nancy L. Moore, Nicole L. |
author_facet | Weigel, Nancy L. Moore, Nicole L. |
author_sort | Weigel, Nancy L. |
collection | PubMed |
description | Although the primary signal for the activation of steroid hormone receptors is binding of hormone, there is increasing evidence that the activities of cell signaling pathways and the phosphorylation status of these transcription factors and their coregulators determine the overall response to the hormone. In some cases, enhanced cell signaling is sufficient to cause activation of receptors in medium depleted of steroids. Steroid receptors are targets for multiple kinases. Many of the phosphorylation sites contain Ser/Thr-Pro motifs implicating proline-directed kinases such as the cyclin-dependent kinases and the mitogen-activated kinases (MAPK) in receptor phosphorylation. Although some sites are constitutively phosphorylated, others are phosphorylated in response to hormone. Still others are only phosphorylated in response to specific cell signaling pathways. Phosphorylation of specific sites has been implicated not only in overall transcriptional activity, but also in nuclear localization, protein stability, and DNA binding. The studies of the roles of phosphorylation in coregulator function are more limited, but it is now well established that many of them are highly phosphorylated and that phosphorylation regulates their function. There is good evidence that some of the phosphorylation sites in the receptors and coregulators are targets of multiple signaling pathways. Individual sites have been associated both with functions that enhance the activity of the receptor, as well as with functions that inhibit activity. Thus, the specific combinations of phosphorylations of the steroid receptor combined with the expression levels and phosphorylation status of coregulators will determine the genes regulated and the biological response. |
format | Text |
id | pubmed-1876600 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | The Nuclear Receptor Signaling Atlas |
record_format | MEDLINE/PubMed |
spelling | pubmed-18766002007-05-24 Kinases and protein phosphorylation as regulators of steroid hormone action Weigel, Nancy L. Moore, Nicole L. Nucl Recept Signal Review Although the primary signal for the activation of steroid hormone receptors is binding of hormone, there is increasing evidence that the activities of cell signaling pathways and the phosphorylation status of these transcription factors and their coregulators determine the overall response to the hormone. In some cases, enhanced cell signaling is sufficient to cause activation of receptors in medium depleted of steroids. Steroid receptors are targets for multiple kinases. Many of the phosphorylation sites contain Ser/Thr-Pro motifs implicating proline-directed kinases such as the cyclin-dependent kinases and the mitogen-activated kinases (MAPK) in receptor phosphorylation. Although some sites are constitutively phosphorylated, others are phosphorylated in response to hormone. Still others are only phosphorylated in response to specific cell signaling pathways. Phosphorylation of specific sites has been implicated not only in overall transcriptional activity, but also in nuclear localization, protein stability, and DNA binding. The studies of the roles of phosphorylation in coregulator function are more limited, but it is now well established that many of them are highly phosphorylated and that phosphorylation regulates their function. There is good evidence that some of the phosphorylation sites in the receptors and coregulators are targets of multiple signaling pathways. Individual sites have been associated both with functions that enhance the activity of the receptor, as well as with functions that inhibit activity. Thus, the specific combinations of phosphorylations of the steroid receptor combined with the expression levels and phosphorylation status of coregulators will determine the genes regulated and the biological response. The Nuclear Receptor Signaling Atlas 2007-05-17 /pmc/articles/PMC1876600/ /pubmed/17525795 http://dx.doi.org/10.1621/nrs.05005 Text en Copyright © 2007, Weigel and Moore. This is an open-access article distributed under the terms of the Creative Commons Non-Commercial Attribution License, which permits unrestricted non-commercial use distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Weigel, Nancy L. Moore, Nicole L. Kinases and protein phosphorylation as regulators of steroid hormone action |
title | Kinases and protein phosphorylation as regulators of steroid hormone action
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title_full | Kinases and protein phosphorylation as regulators of steroid hormone action
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title_fullStr | Kinases and protein phosphorylation as regulators of steroid hormone action
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title_full_unstemmed | Kinases and protein phosphorylation as regulators of steroid hormone action
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title_short | Kinases and protein phosphorylation as regulators of steroid hormone action
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title_sort | kinases and protein phosphorylation as regulators of steroid hormone action |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1876600/ https://www.ncbi.nlm.nih.gov/pubmed/17525795 http://dx.doi.org/10.1621/nrs.05005 |
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