Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins.

Détails

ID Serval
serval:BIB_9015AC855B03
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins.
Périodique
European journal of biochemistry / FEBS
Auteur(s)
Corti C., Leclerc L'Hostis E., Quadroni M., Schmid H., Durussel I., Cox J., Dainese Hatt P., James P., Carafoli E.
ISSN
0014-2956
Statut éditorial
Publié
Date de publication
06/1999
Peer-reviewed
Oui
Volume
262
Numéro
3
Pages
790-802
Langue
anglais
Résumé
The activation of six target enzymes by calmodulin phosphorylated on Tyr99 (PCaM) and the binding affinities of their respective calmodulin binding domains were tested. The six enzymes were: myosin light chain kinase (MLCK), 3'-5'-cyclic nucleotide phosphodiesterase (PDE), plasma membrane (PM) Ca2+-ATPase, Ca2+-CaM dependent protein phosphatase 2B (calcineurin), neuronal nitric oxide synthase (NOS) and type II Ca2+-calmodulin dependent protein kinase (CaM kinase II). In general, tyrosine phosphorylation led to an increase in the activatory properties of calmodulin (CaM). For plasma membrane (PM) Ca2+-ATPase, PDE and CaM kinase II, the primary effect was a decrease in the concentration at which half maximal velocity was attained (Kact). In contrast, for calcineurin and NOS phosphorylation of CaM significantly increased the Vmax. For MLCK, however, neither Vmax nor Kact were affected by tyrosine phosphorylation. Direct determination by fluorescence techniques of the dissociation constants with synthetic peptides corresponding to the CaM-binding domain of the six analysed enzymes revealed that phosphorylation of Tyr99 on CaM generally increased its affinity for the peptides.
Mots-clé
3',5'-Cyclic-AMP Phosphodiesterases, Amino Acid Sequence, Animals, Binding, Competitive, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases, Calcium-Transporting ATPases, Calmodulin, Cattle, Chickens, Fluorescent Dyes, Kinetics, Molecular Sequence Data, Myosin-Light-Chain Kinase, Nitric Oxide Synthase, Nitric Oxide Synthase Type I, Peptides, Phosphorylation, Proteins, Substrate Specificity, Tyrosine, src-Family Kinases
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:46
Dernière modification de la notice
08/05/2019 21:57
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