Domain II of calmodulin is involved in activation of calcineurin

FEBS Lett. 1988 Sep 26;238(1):82-6. doi: 10.1016/0014-5793(88)80230-8.


A family of mutant proteins related to calmodulin (CaM) has been produced using cDNA constructs in bacterial expression vectors. The new proteins contain amino acid substitutions in Ca2+-binding domains I, II, both I and II, or both II and IV. The calmodulin-like proteins have been characterized with respect to mobility on SDS-polyacrylamide gels, Ca2+-dependent enhancement of tyrosine fluorescence, and abilities to activate the CaM-dependent phosphatase calcineurin. These studies suggest that an intact Ca2+-binding domain II is minimally required for full activation of calcineurin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Calcineurin
  • Calmodulin / genetics
  • Calmodulin / physiology*
  • Calmodulin-Binding Proteins / metabolism*
  • Chickens
  • Enzyme Activation
  • Genes
  • Genetic Vectors
  • Phosphoprotein Phosphatases / metabolism*
  • Pseudogenes


  • Calmodulin
  • Calmodulin-Binding Proteins
  • Calcineurin
  • Phosphoprotein Phosphatases