Related Experiment Video
Updated: Jun 24, 2026

In Vitro Bioluminescence Assay to Characterize Circadian Rhythm in Mammary Epithelial Cells
Published on: September 28, 2017
CK2alpha phosphorylates BMAL1 to regulate the mammalian clock
Teruya Tamaru1, Jun Hirayama, Yasushi Isojima
1Department of Physiology, Toho University School of Medicine, Tokyo, Japan.
Abstract:
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.
Related Concept Videos
Circadian Rhythms and Gene Regulation
Circadian Rhythms and Gene Regulation
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Positive Regulator Molecules
Positive Regulator Molecules
Biological Clocks and Seasonal Responses

