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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 |
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| 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
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| Schlagwörter: |
| Zusammenfassung: | <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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| Umfang: | 5921-5925 |
| ISSN: |
0027-8424
1091-6490 |
| DOI: | 10.1073/pnas.81.19.5921 |