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The Journal of Neuroscience, November 30, 2005, 25(48):11175-11183; doi:10.1523/JNEUROSCI.2159-05.2005
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Cellular/Molecular
In Vivo Circadian Function of Casein Kinase 2 Phosphorylation Sites in Drosophila PERIOD
Jui-Ming Lin,
Analyne Schroeder, and
Ravi Allada
Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208
Phosphorylation plays a key role in the precise timing of circadian clocks. Daily rhythms of phosphorylation of the Drosophila circadian clock component PERIOD (PER) were first described more than a decade ago, yet little is known about their phosphorylation sites and their function in circadian behavior. Here we show that serines 151 and 153 in PER are required for robust in vitro phosphorylation by the casein kinase 2 (CK2) holoenzyme, a cytoplasmic kinase shown to be involved in circadian rhythms. Mutation of these sites in transgenic flies results in significant period lengthening of behavioral rhythms, altered PER rhythms, and delayed PER nuclear localization in circadian pacemaker neurons. In many respects, mutation of these phosphorylation sites phenocopies mutation of the catalytic subunit of CK2. We propose that CK2 phosphorylation at these sites triggers PER nuclear localization.
Key words: Drosophila; phosphorylation; CK2; PERIOD; circadian clock; holoenzyme; pacemaker neuron
Received May 27, 2005;
revised October 15, 2005;
accepted October 18, 2005.
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