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. 1999 Dec 1;344(Pt 2):403–411.

Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymes.

E Leclerc 1, C Corti 1, H Schmid 1, S Vetter 1, P James 1, E Carafoli 1
PMCID: PMC1220657  PMID: 10567222

Abstract

The interaction of serine/threonine-phosphorylated calmodulin with synthetic peptides corresponding to the calmodulin-binding domains of six enzymes has been studied by fluorescence spectroscopy. For five peptides, the dissociation constant of the calmodulin-peptide complex (K(d)) increased when calmodulin was phosphorylated. An increase of more than one order of magnitude was observed with peptides derived from smooth-muscle myosin light-chain kinase and cAMP phosphodiesterase. In contrast, only a slight increase in K(d) was noted with two peptides derived from the plasma membrane Ca(2+)-ATPase and for the peptide derived from nitric oxide synthase. No significant change in affinity was detected with the peptide derived from calcineurin. In contrast, a decrease in the dissociation constant was observed with the peptide derived from the Ca(2+)-calmodulin dependent kinase II. Phosphorylation also affected the peptide-calmodulin binding stoichiometry: a decrease from two to one binding sites was observed with the peptides derived from myosin light-chain kinase and phosphodiesterase.

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Selected References

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