Interactive Features of Proteins Composing Eukaryotic Circadian Clocks

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 str...

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Bibliographic Details
Published in:Annual review of biochemistry 2014-01, Vol.83 (1), p.191-219
Main Authors: Crane, Brian R, Young, Michael W
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Cattle
Circadian Clocks - physiology
Circadian rhythm
Circadian Rhythm - physiology
Circadian rhythms
CLOCK Proteins - physiology
Drosophila
Eukaryotes
Fungi - physiology
Glycosylation
Humans
Insecta - physiology
Light
metabolism
PAS domain
Phosphorylation
Photochemistry - methods
photoentrainment
Protein Binding
Protein Conformation
Protein Interaction Mapping
Protein Processing, Post-Translational
Proteins
Rhodopsin - physiology
Rod Opsins - physiology
Signal Transduction
Transcription, Genetic
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Summary: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.
ISSN:0066-4154
1545-4509
DOI:10.1146/annurev-biochem-060713-035644