Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 83
Volume 83, Issue -, Pages 191-219Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060713-035644
Keywords
circadian rhythm; phosphorylation; glycosylation; metabolism; PAS domain; photoentrainment
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Funding
- NIGMS NIH HHS [R37 GM054339, GM079679, GM054339, R01 GM079679] Funding Source: Medline
- NINDS NIH HHS [NS053087, R01 NS053087] Funding Source: Medline
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Research into the molecular mechanisms of eukaryotic circadian clocks has proceeded at an electrifying pace. In this review, we discuss advances in our understanding of the structures of central molecular players in the timing oscillators of fungi, insects, and mammals. A series of clock protein structures demonstrate that the PAS (Per/Arnt/Sim) domain has been used with great variation to formulate the transcriptional activators and repressors of the clock. We discuss how posttranslational modifications and external cues, such as light, affect the conformation and function of core clock components. Recent breakthroughs have also revealed novel interactions among clock proteins and new partners that couple the clock to metabolic and developmental pathways. Overall, a picture of clock function has emerged wherein conserved motifs and structural platforms have been elaborated into a highly dynamic collection of interacting molecules that undergo orchestrated changes in chemical structure, conformational state, and partners.
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