Domain II of calmodulin is involved in activation of calcineurin

FEBS Letters

Klee, Claude B.²  Putkey, John A.¹  Means, Anthony R.¹  Hurwitz, Mary Y.¹ 

[1] Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030 USA;NCI, NIH, Bethesda, MD 20892, USA

关键词: Calmodulin;    Calcineurin;    Mutagenesis;   

DOI  :  10.1016/0014-5793(88)80230-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown