Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 16, Issue 4, Pages 446-448Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1578
Keywords
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Funding
- Human Frontiers in Science Program Organization
- Japanese Ministry of Education, Culture, Sports, Science and Technology
- Cancer Research Coordinating Committee of the University of California
- US National Institutes of Health
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Clock proteins govern circadian physiology and their function is regulated by various mechanisms. Here we demonstrate that Casein kinase (CK)-2 alpha phosphorylates the core circadian regulator BMAL1. Gene silencing of CK2 alpha or mutation of the highly conserved CK2-phosphorylation site in BMAL1, Ser90, result in impaired nuclear BMAL1 accumulation and disruption of clock function. Notably, phosphorylation at Ser90 follows a rhythmic pattern. These findings reveal that CK2 is an essential regulator of the mammalian circadian system.
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