Direct evidence of in vitro phosphorylation-dephosphorylation of the estradiol-17β receptor. role of Ca2+-Calmodulin in the activation of hormone binding sites

Ferdinando Auricchio, Antimo Migliaccio, Gabriella Castoria, Andrea Rotondi, Secondo Lastoria

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The calf uterus estradiol-17β receptor is a phosphoprotein and its hormone binding activity is regulated by two endogenous enzymes both of which have been purified and characterized in detail: a nuclear phosphatase that inactivates the hormone binding sites of the receptor, and a cytosol kinase that activates these sites. Here we report that the kinase is stimulated by Ca2+ and calmodulin. Direct evidence is presented that the receptor is phosphorylated by the kinase and dephosphorylated by the phosphatase.

Original languageEnglish
Pages (from-to)31-35
Number of pages5
JournalJournal of Steroid Biochemistry
Volume20
Issue number1
DOIs
Publication statusPublished - 1984

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Estradiol Receptors
Phosphorylation
Calmodulin
Estradiol
Phosphotransferases
Chemical activation
Binding Sites
Hormones
Phosphoric Monoester Hydrolases
Phosphoproteins
Cytosol
Uterus
Enzymes
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

Direct evidence of in vitro phosphorylation-dephosphorylation of the estradiol-17β receptor. role of Ca2+-Calmodulin in the activation of hormone binding sites. / Auricchio, Ferdinando; Migliaccio, Antimo; Castoria, Gabriella; Rotondi, Andrea; Lastoria, Secondo.

In: Journal of Steroid Biochemistry, Vol. 20, No. 1, 1984, p. 31-35.

Research output: Contribution to journalArticle

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