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Citation
Maurer, C., Hung, H.C., Weber, F. (2009). Cytoplasmic interaction with CYCLE promotes the post-translational processing of the circadian CLOCK protein.  FEBS Lett. 583(10): 1561--1566.
FlyBase ID
FBrf0208031
Publication Type
Research paper
Abstract
Post-translational regulation of the transcription factor CLOCK (CLK) is crucial for circadian clock function. The contribution of the hetero-dimerization partner CYCLE (CYC) to the post-translational regulation of CLK is largely unknown. Here we report that Drosophila CLK and CYC proteins not only interact in the nucleus, where they activate circadian transcription, but also in the cytoplasm of Drosophila S2R+ cells. Cytoplasmic CLK accumulates in a hypo-phosphorylated state. Impairment of CYC-binding caused a further reduction in CLK phosphorylation, while over-expression of CYC enhanced the phosphorylation of cytoplasmic CLK towards a hypo-phosphorylated state. CYC also promotes nuclear import of CLK, which is required for hyper-phosphorylation of the CLK protein. Our results indicate a role of CYC in the post-translational regulation of the CLK protein.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    FEBS Lett.
    Title
    FEBS Letters
    Publication Year
    1968-
    ISBN/ISSN
    0014-5793
    Data From Reference
    Genes (2)
    Physical Interactions (1)
    Cell Lines (1)