Phosphorylation of calcineurin: Effect on calmodulin binding

Mihail B. Calalb, Randall L. Kincaid, Thomas R. Soderling

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The effect of phosphorylation of calcineurin on calmodulin (CaM) binding was examined using a synthetic peptide which contains the CaM-binding domain and the serine phosphorylation site. The peptide, corresponding to residues 391-414 of brain calcineurin A subunit, was rapidly phosphorylated by protein kinase C and Ca2+ CaM-dependent protein kinase II but not by cAMP-dependent protein kinase. Phosphorylation of peptide 391-414 did not significantly alter the binding of CaM when compared to the non-phosphorylated peptide.

Original languageEnglish (US)
Pages (from-to)551-556
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume172
Issue number2
DOIs
StatePublished - Oct 30 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Phosphorylation of calcineurin: Effect on calmodulin binding'. Together they form a unique fingerprint.

Cite this