Domain II of calmodulin is involved in activation of calcineurin.
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.
Hurwitz
M Y
MY
Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.
Putkey
J A
JA
Klee
C B
CB
Means
A R
AR
D000818:Animals; D019703:Calcineurin; D002147:Calmodulin / Q000235:genetics / Q000502:physiology*; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002645:Chickens; D004789:Enzyme Activation; D005796:Genes; D005822:Genetic Vectors; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D011544:Pseudogenes
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases