Domain II of calmodulin is involved in activation of calcineurin.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Hurwitz, MY; Putkey, JA; Klee, CB; Means, AR

Published Date

  • September 26, 1988

Published In

Volume / Issue

  • 238 / 1

Start / End Page

  • 82 - 86

PubMed ID

  • 2844597

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(88)80230-8


  • eng

Conference Location

  • England