Abstract
Drosophila ninaC gene encodes myosin homologous proteins which are classified as myosin III of the myosin superfamily, yet the physiological and biochemical function of myosin III has not characterized. We report here that myosin III does exhibit protein kinase activity. The kinase homologous domain (MYOIIIPK) of myosin III was expressed in the baculovirus expression system and purified to homogeneity. MYOIIIPK phosphorylated a number of proteins including myosin III p132 and smooth muscle myosin regulatory light chain (LC20), suggesting that myosin III is a multifunctional protein kinase. The phosphoamino acid analysis revealed that myosin III is a serine/threonine kinase but not a tyrosine kinase. The observation that MYOIIIPK phosphorylates myosin III suggests that the autophosphorylation might play a role for the regulation of myosin III function. This is the first direct demonstration of kinase activity for the myosin III class.
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