ArticleMolecular and cellular biology2004
Drosophila doubletime mutations which either shorten or lengthen the period of circadian rhythms decrease the protein kinase activity of casein kinase I.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 82 citations in OpenAlex.
- Article
- Post-Translational Modifications in Animal Circadian Clocks.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Molecular genetic characterization ofbioRxiv : the preprint server for biology · 2025Article
- A wrinkle in timers: evolutionary rewiring of conserved biological timekeepers.Trends in biochemical sciences · 2025Review
- Clock gene homologs lin-42 and kin-20 regulate circadian rhythms in C. elegans.Scientific reports · 2024Article
- Decoupling PER phosphorylation, stability and rhythmic expression from circadian clock function by abolishing PER-CK1 interaction.Nature communications · 2022Article
- Kinase domain autophosphorylation rewires the activity and substrate specificity of CK1 enzymes.Molecular cell · 2022Article
- Article
- FRQ-CK1 interaction determines the period of circadian rhythms in Neurospora.Nature communications · 2019Article
- A Symphony of Signals: Intercellular and Intracellular Signaling Mechanisms Underlying Circadian Timekeeping in Mice and Flies.International journal of molecular sciences · 2019Review
- The CircadianInternational journal of molecular sciences · 2019Article
- Coordination between Differentially Regulated Circadian Clocks Generates Rhythmic Behavior.Cold Spring Harbor perspectives in biology · 2018Review
- Reflections on contributing to "big discoveries" about the fly clock: Our fortunate paths as post-docs with 2017 Nobel laureates Jeff Hall, Michael Rosbash, and Mike Young.Neurobiology of sleep and circadian rhythms · 2018Review
- Article
- Correlated evolution between CK1δ Protein and the Serine-rich Motif Contributes to Regulating the Mammalian Circadian Clock.The Journal of biological chemistry · 2017Article
- Codon usage affects the structure and function of the Drosophila circadian clock protein PERIOD.Genes & development · 2016Article
- Identification of Evening Complex Associated Proteins in Arabidopsis by Affinity Purification and Mass Spectrometry.Molecular & cellular proteomics : MCP · 2016Article
- A Doubletime Nuclear Localization Signal Mediates an Interaction with Bride of Doubletime to Promote Circadian Function.Journal of biological rhythms · 2015Article
- Drosophila DBT Autophosphorylation of Its C-Terminal Domain Antagonized by SPAG and Involved in UV-Induced Apoptosis.Molecular and cellular biology · 2015Article
- Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
In both mammals and fruit flies, casein kinase I has been shown to regulate the circadian phosphorylation of the period protein (PER). This phosphorylation regulates the timing of PER's nuclear accumulation and decline, and it is necessary for the generation of circadian rhythms. In Drosophila melanogaster, mutations affecting a casein kinase I (CKI) ortholog called doubletime (dbt) can produce short or long periods. The effects of both a short-period (dbt(S)) and long-period (dbt(L)) mutation on DBT expression and biochemistry were analyzed. Immunoblot analysis of DBT in fly heads showed that both the dbt(S) and dbt(L) mutants express DBT at constant levels throughout the day. Glutathione S-transferase pull-down assays and coimmunoprecipitation of DBT and PER showed that wild-type DBT, DBT(S), and DBT(L) proteins can bind to PER equivalently and that these interactions are mediated by the evolutionarily conserved N-terminal part of DBT. However, both the dbt(S) and dbt(L) mutations reduced the CKI-7-sensitive kinase activity of an orthologous Xenopus laevis CKIdelta expressed in Escherichia coli. Moreover, expression of DBT in Drosophila S2 cells produced a CKI-7-sensitive kinase activity which was reduced by both the dbt(S) and dbt(L) mutations. Thus, lowered enzyme activity is associated with both short-period and long-period phenotypes.
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