Phosphorylation of PERIOD is influenced by cycling physical associations of DOUBLE-TIME, PERIOD, and TIMELESS in the Drosophila clock

Brian Kloss, Adrian Rothenfluh, Michael W. Young, Lino Saez

Research output: Contribution to journalArticlepeer-review

156 Scopus citations

Abstract

The clock gene double-time (dbt) encodes an ortholog of casein kinase Iε that promotes phosphorylation and turnover of the PERIOD protein. Whereas the period (per), timeless (tim), and dClock (dClk) genes of Drosophila each contribute cycling mRNA and protein to a circadian clock, dbt RNA and DBT protein are constitutively expressed. Robust circadian changes in DBT subcellular localization are nevertheless observed in clock-containing cells of the fly head. These localization rhythms accompany formation of protein complexes that include PER, TIM, and DBT, and reflect periodic redistribution between the nucleus and the cytoplasm. Nuclear phosphorylation of PER is strongly enhanced when TIM is removed from PER/TIM/DBT complexes. The varying associations of PER, DBT and TIM appear to determine the onset and duration of nuclear PER function within the Drosophila clock.

Original languageEnglish (US)
Pages (from-to)699-706
Number of pages8
JournalNeuron
Volume30
Issue number3
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • General Neuroscience

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