Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The phospho-occupancy of an atypical SLIMB-binding site on PERIOD that is phosphorylated by DOUBLETIME controls the pace of the clock.

Genes & development - 1 Jul 2008

Chiu Joanna C, Vanselow Jens T, Kramer Achim, Edery Isaac

Abstract excerpt

A common feature of animal circadian clocks is the progressive phosphorylation of PERIOD (PER) proteins, which is highly dependent on casein kinase Idelta/epsilon (CKIdelta/epsilon; termed DOUBLETIME [DBT] in Drosophila) and ultimately leads to the rapid degradation of hyperphosphorylated isoforms via a mechanism involving the F-box protein, beta-TrCP (SLIMB in Drosophila). Here we use the Drosophila melanogaster...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Cycle Proteins
Share to Circadian Rhythm

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drosophila melanogaster

Share to Drosophila Proteins

Share to Mass Spectrometry

Share to Period Circadian Proteins

Share to Phosphorylation

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 18593878
DOI: 10.1101/gad.1682708
PMCID: PMC2492663

Genes

DBT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The phospho-occupancy of an atypical SLIMB-binding site on PERIOD that is phosphorylated by DOUBLETIME controls the pace of the clock.PMID 18593878Read ↗

Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime.Semantic proximity Read ↗

PERspective on PER phosphorylation.Semantic proximity Read ↗

Identification of Light-Sensitive Phosphorylation Sites on PERIOD That Regulate the Pace of Circadian Rhythms in Drosophila.Semantic proximity Read ↗

Drosophila doubletime mutations which either shorten or lengthen the period of circadian rhythms decrease the protein kinase activity of casein kinase I.Semantic proximity Read ↗

The dramatic impact of the PER-DBT interaction on circadian timekeeping and temperature compensationSemantic proximity Read ↗

Cooperative interaction between phosphorylation sites on PERIOD maintains circadian period in Drosophila.Semantic proximity Read ↗

Activating PER repressor through a DBT-directed phosphorylation switch.Semantic proximity Read ↗

The F-box protein slimb controls the levels of clock proteins period and timeless.Semantic proximity Read ↗

Essential roles of CKIdelta and CKIepsilon in the mammalian circadian clock.Semantic proximity Read ↗

A role for casein kinase 2alpha in the Drosophila circadian clock.Semantic proximity Read ↗

Casein kinase I: another cog in the circadian clockworks.Semantic proximity Read ↗

Drosophila and vertebrate casein kinase Idelta exhibits evolutionary conservation of circadian function.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.