CK2alpha phosphorylates BMAL1 to regulate the mammalian clock

Nat Struct Mol Biol. 2009 Apr;16(4):446-8. doi: 10.1038/nsmb.1578. Epub 2009 Mar 29.


Clock proteins govern circadian physiology and their function is regulated by various mechanisms. Here we demonstrate that Casein kinase (CK)-2alpha phosphorylates the core circadian regulator BMAL1. Gene silencing of CK2alpha 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • ARNTL Transcription Factors
  • Basic Helix-Loop-Helix Transcription Factors / genetics
  • Basic Helix-Loop-Helix Transcription Factors / metabolism*
  • Biological Clocks*
  • Casein Kinase II / genetics
  • Casein Kinase II / metabolism*
  • Cell Nucleus / chemistry
  • Gene Silencing
  • Mutagenesis, Site-Directed
  • Phosphorylation


  • ARNTL Transcription Factors
  • Basic Helix-Loop-Helix Transcription Factors
  • Casein Kinase II