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. 1984 Oct;81(19):5921–5925. doi: 10.1073/pnas.81.19.5921

Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine.

A Migliaccio, A Rotondi, F Auricchio
PMCID: PMC391830  PMID: 6207535

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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