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


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
Issue number1
Publication statusPublished - 1984


ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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