DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping.

@article{Kurabayashi2010DYRK1AAG,
  title={DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping.},
  author={Nobuhiro Kurabayashi and Tsuyoshi Hirota and Mihoko Sakai and Kamon Sanada and Yoshitaka Fukada},
  journal={Molecular and cellular biology},
  year={2010},
  volume={30 7},
  pages={1757-68}
}
Circadian molecular oscillation is generated by a transcription/translation-based feedback loop in which CRY proteins play critical roles as potent inhibitors for E-box-dependent clock gene expression. Although CRY2 undergoes rhythmic phosphorylation in its C-terminal tail, structurally distinct from the CRY1 tail, little is understood about how protein kinase(s) controls the CRY2-specific phosphorylation and contributes to the molecular clockwork. Here we found that Ser557 in the C-terminal… CONTINUE READING

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