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Lim, Chunghun
Neurogenetics & Ribonomics Laboratory (The Lim Lab)
Research Interests
  • Ribosome Biology, Translation, Neurodegeneration, Behavioral Genetics

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The DOUBLETIME protein kinase regulates phosphorylation of the Drosophila PDP1 epsilon

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Title
The DOUBLETIME protein kinase regulates phosphorylation of the Drosophila PDP1 epsilon
Author
Choi, ChangtaekLee, JongbinLim, ChunghunJang, DonghoonChoe, Joonho
Issue Date
2009-10
Publisher
WILEY-BLACKWELL
Citation
JOURNAL OF NEUROCHEMISTRY, v.111, no.1, pp.264 - 273
Abstract
Reversible phosphorylation of clock proteins plays an important role in circadian timekeeping as it is a key post-translational mechanism that regulates the activity, stability and subcellular localization of core clock proteins. The kinase DOUBLETIME (DBT), a Drosophila ortholog of mammalian casein kinase I epsilon, regulates circadian phosphorylation of two essential clock proteins, PERIOD and dCLOCK. We present evidence that Par Domain Protein 1 epsilon (PDP1 epsilon), a transcription factor and mediator of clock output in Drosophila, is phosphorylated in vivo and in cultured cells by DBT activity. We also demonstrate that DBT interacts with PDP1 epsilon and promotes its degradation by the ubiquitin-proteasome pathway in cultured cells. In addition, PDP1 epsilon nuclear localization is decreased by dbt RNA interference in S2 cell system. These results suggest that DBT regulates phosphorylation, stability and localization of PDP1 epsilon, and that it has multiple targets in the Drosophila circadian system.
URI
https://scholarworks.unist.ac.kr/handle/201301/9828
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=70349214768
DOI
10.1111/j.1471-4159.2009.06327.x
ISSN
0022-3042
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BIO_Journal Papers
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