Calmodulin has the Potential to Function as a Ca-Dependent Adaptor Protein.

ABSTRACT: Calmodulin (CaM) is a versatile Ca(2+)-binding protein that regulates the activity of numerous effector proteins in response to Ca(2+) signals. Several CaM-dependent regulatory mechanisms have been identified, including autoinhibitory domain displacement, sequestration of a ligand-binding site, active site reorganization, and target protein dimerization. We recently showed that the N- and C-lobes of animal and plant CaM isoforms could independently and sequentially bind to target peptides derived from the CaM-binding domain of Nicotiana tabacum mitogen-activated protein kinase phosphatase (NtMKP1), to form a 2:1 peptide:CaM complex. This suggests that CaM might facilitate the dimerization of NtMKP1, although the dimerization mechanism is distinct from the previously described simultaneous

SUBMITTER: Yamniuk AP 

PROVIDER: S-EPMC2634210 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature