Phosphorylation of calcineurin: Effect on calmodulin binding

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

Research output: Contribution to journalArticle

10 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Phosphorylation
Calcineurin
Calmodulin
Peptides
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Cyclic AMP-Dependent Protein Kinases
Serine
Protein Kinase C
Brain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of calcineurin : Effect on calmodulin binding. / Calalb, Mihail B.; Kincaid, Randall L.; Soderling, Thomas.

In: Biochemical and Biophysical Research Communications, Vol. 172, No. 2, 30.10.1990, p. 551-556.

Research output: Contribution to journalArticle

Calalb, Mihail B. ; Kincaid, Randall L. ; Soderling, Thomas. / Phosphorylation of calcineurin : Effect on calmodulin binding. In: Biochemical and Biophysical Research Communications. 1990 ; Vol. 172, No. 2. pp. 551-556.
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