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Domain II of calmodulin is involved in activation of calcineurin
Author(s) -
Hurwitz Mary Y.,
Putkey John A.,
Klee Claude B.,
Means Anthony R.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80230-8
Subject(s) - calcineurin , calmodulin , domain (mathematical analysis) , chemistry , calmodulin binding proteins , microbiology and biotechnology , computational biology , biochemistry , biology , medicine , mathematics , enzyme , transplantation , mathematical analysis
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 Ca 2+ ‐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, Ca 2+ ‐dependent enhancement of tyrosine fluorescence, and abilities to activate the CaM‐dependent phosphatase calcineurin. These studies suggest that an intact Ca 2+ ‐binding domain II is minimally required for full activation of calcineurin.