Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime

@article{Ko2002RoleFS,
  title={Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime},
  author={H. Ko and J. Jiang and I. Edery},
  journal={Nature},
  year={2002},
  volume={420},
  pages={673-678}
}
Protein phosphorylation has a key role in modulating the stabilities of circadian clock proteins in a manner specific to the time of day. A conserved feature of animal clocks is that Period (Per) proteins undergo daily rhythms in phosphorylation and levels, events that are crucial for normal clock progression. Casein kinase Iε (CKIε) has a prominent role in regulating the phosphorylation and abundance of Per proteins in animals. This was first shown in Drosophila with the characterization of… Expand
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323 Citations
Highly Influential Citations
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Background Citations
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Methods Citations
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Results Citations
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323 Citations

Citation Type

Citation Type

The DOUBLETIME protein kinase regulates phosphorylation of the Drosophila PDP1ε
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Balance between DBT/CKIepsilon kinase and protein phosphatase activities regulate phosphorylation and stability of Drosophila CLOCK protein.
  • E. Kim, I. Edery
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
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  • 142
  • PDF
Analyzing the degradation of PERIOD protein by the ubiquitin-proteasome pathway in cultured Drosophila cells.
  • 9
A DOUBLETIME Kinase Binding Domain on the Drosophila PERIOD Protein Is Essential for Its Hyperphosphorylation, Transcriptional Repression, and Circadian Clock Function
  • 102
  • PDF
Ribosomal S6 Kinase Cooperates with Casein Kinase 2 to Modulate the Drosophila Circadian Molecular Oscillator
  • 32
  • PDF
Activating PER Repressor through a DBT-Directed Phosphorylation Switch
  • 81
  • PDF
The phospho-occupancy of an atypical SLIMB-binding site on PERIOD that is phosphorylated by DOUBLETIME controls the pace of the clock.
  • 134
  • PDF
Control of Mammalian Circadian Rhythm by CKIε-Regulated Proteasome-Mediated PER2 Degradation
  • 382
  • Highly Influenced
  • PDF
Kinetics of Doubletime Kinase-dependent Degradation of the Drosophila Period Protein*
  • 37
  • PDF
The proteasome-dependent degradation of CKB4 is regulated by the Arabidopsis biological clock.
  • 72
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