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J Biol Chem, Vol. 274, Issue 53, 37821-37826, December 31, 1999

Ca²⁺/Calmodulin-independent Activation of Calcineurin from Dictyostelium by Unsaturated Long Chain Fatty Acids^*

Ursula Kessen, Ralph Schaloske, Annette Aichem, and Rupert Mutzel

From the Fakultät für Biologie, Universität Konstanz, D-78457 Konstanz, Germany

This study describes a novel mode of activation for the Ca²⁺/calmodulin-dependent protein phosphatase calcineurin. Using purified calcineurin from Dictyostelium discoideum we found a reversible, Ca²⁺/calmodulin-independent activation by the long chain unsaturated fatty acids arachidonic acid, linoleic acid, and oleic acid, which was of the same magnitude as activation by Ca²⁺/calmodulin. Half-maximal stimulation of calcineurin occurred at fatty acid concentrations of approximately 10 µM with either p-nitrophenyl phosphate or RII phosphopeptide as substrates. The methyl ester of arachidonic acid and the saturated fatty acids palmitic acid and arachidic acid did not activate calcineurin. The activation was shown to be independent of the regulatory subunit, calcineurin B. Activation by Ca²⁺/calmodulin and fatty acids was not additive. In binding assays with immobilized calmodulin, arachidonic acid inhibited binding of calcineurin to calmodulin. Therefore fatty acids appear to mimic Ca²⁺/calmodulin action by binding to the calmodulin-binding site.

This work is dedicated to Professor Dieter Malchow on the occasion of his 60th birthday.

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