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Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine.
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Proceedings of the National Academy of Sciences, 81, 1984, 19, S. 5921-5925 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Migliaccio, A Rotondi, A Auricchio, F Migliaccio, A Rotondi, A Auricchio, F |
|---|---|
| author |
Migliaccio, A Rotondi, A Auricchio, F |
| spellingShingle |
Migliaccio, A Rotondi, A Auricchio, F Proceedings of the National Academy of Sciences Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. Multidisciplinary |
| author_sort |
migliaccio, a |
| spelling |
Migliaccio, A Rotondi, A Auricchio, F 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.81.19.5921 <jats:p>The calf uterine 17 beta-estradiol receptor is a phosphoprotein. Phosphorylation-dephosphorylation of the receptor is controlled by a cytosol receptor kinase that activates the hormone binding and by a nuclear phosphatase that inactivates this binding. This report concerns the nature of the 17 beta-estradiol receptor kinase. Highly purified calf uterus 17 beta-estradiol receptor preinactivated by the nuclear phosphatase was used as substrate of the purified receptor kinase. Ca2+ and calmodulin stimulate both the kinase-dependent activation of the hormone binding and 32P incorporation from [gamma-32P]-ATP into the receptor. Maximal stimulation of hormone binding activation requires 1 microM Ca2+ and 0.6 microM calmodulin. Fifteen micromolar trifluoperazine is the lowest concentration that will prevent completely Ca2+-calmodulin stimulation of the kinase. The receptor is phosphorylated by the receptor kinase exclusively on tyrosine. Phosphorylation of proteins on tyrosine is a rare event implicated in hormone-induced cell growth and cell transformation.</jats:p> Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. Proceedings of the National Academy of Sciences |
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Proceedings of the National Academy of Sciences, 1984 |
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| title |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_unstemmed |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_full |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_fullStr |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_full_unstemmed |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_short |
Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_sort |
calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.81.19.5921 |
| publishDate |
1984 |
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5921-5925 |
| description |
<jats:p>The calf uterine 17 beta-estradiol receptor is a phosphoprotein. Phosphorylation-dephosphorylation of the receptor is controlled by a cytosol receptor kinase that activates the hormone binding and by a nuclear phosphatase that inactivates this binding. This report concerns the nature of the 17 beta-estradiol receptor kinase. Highly purified calf uterus 17 beta-estradiol receptor preinactivated by the nuclear phosphatase was used as substrate of the purified receptor kinase. Ca2+ and calmodulin stimulate both the kinase-dependent activation of the hormone binding and 32P incorporation from [gamma-32P]-ATP into the receptor. Maximal stimulation of hormone binding activation requires 1 microM Ca2+ and 0.6 microM calmodulin. Fifteen micromolar trifluoperazine is the lowest concentration that will prevent completely Ca2+-calmodulin stimulation of the kinase. The receptor is phosphorylated by the receptor kinase exclusively on tyrosine. Phosphorylation of proteins on tyrosine is a rare event implicated in hormone-induced cell growth and cell transformation.</jats:p> |
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| author | Migliaccio, A, Rotondi, A, Auricchio, F |
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| description | <jats:p>The calf uterine 17 beta-estradiol receptor is a phosphoprotein. Phosphorylation-dephosphorylation of the receptor is controlled by a cytosol receptor kinase that activates the hormone binding and by a nuclear phosphatase that inactivates this binding. This report concerns the nature of the 17 beta-estradiol receptor kinase. Highly purified calf uterus 17 beta-estradiol receptor preinactivated by the nuclear phosphatase was used as substrate of the purified receptor kinase. Ca2+ and calmodulin stimulate both the kinase-dependent activation of the hormone binding and 32P incorporation from [gamma-32P]-ATP into the receptor. Maximal stimulation of hormone binding activation requires 1 microM Ca2+ and 0.6 microM calmodulin. Fifteen micromolar trifluoperazine is the lowest concentration that will prevent completely Ca2+-calmodulin stimulation of the kinase. The receptor is phosphorylated by the receptor kinase exclusively on tyrosine. Phosphorylation of proteins on tyrosine is a rare event implicated in hormone-induced cell growth and cell transformation.</jats:p> |
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| imprint | Proceedings of the National Academy of Sciences, 1984 |
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| institution | DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3 |
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| physical | 5921-5925 |
| publishDate | 1984 |
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| spelling | Migliaccio, A Rotondi, A Auricchio, F 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.81.19.5921 <jats:p>The calf uterine 17 beta-estradiol receptor is a phosphoprotein. Phosphorylation-dephosphorylation of the receptor is controlled by a cytosol receptor kinase that activates the hormone binding and by a nuclear phosphatase that inactivates this binding. This report concerns the nature of the 17 beta-estradiol receptor kinase. Highly purified calf uterus 17 beta-estradiol receptor preinactivated by the nuclear phosphatase was used as substrate of the purified receptor kinase. Ca2+ and calmodulin stimulate both the kinase-dependent activation of the hormone binding and 32P incorporation from [gamma-32P]-ATP into the receptor. Maximal stimulation of hormone binding activation requires 1 microM Ca2+ and 0.6 microM calmodulin. Fifteen micromolar trifluoperazine is the lowest concentration that will prevent completely Ca2+-calmodulin stimulation of the kinase. The receptor is phosphorylated by the receptor kinase exclusively on tyrosine. Phosphorylation of proteins on tyrosine is a rare event implicated in hormone-induced cell growth and cell transformation.</jats:p> Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. Proceedings of the National Academy of Sciences |
| spellingShingle | Migliaccio, A, Rotondi, A, Auricchio, F, Proceedings of the National Academy of Sciences, Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine., Multidisciplinary |
| title | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_full | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_fullStr | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_full_unstemmed | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_short | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_sort | calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| title_unstemmed | Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine. |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.81.19.5921 |