Ontology highlight
ABSTRACT:
SUBMITTER: Tamaru T
PROVIDER: S-EPMC6501789 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Tamaru Teruya T Hirayama Jun J Isojima Yasushi Y Nagai Katsuya K Norioka Shigemi S Takamatsu Ken K Sassone-Corsi Paolo P
Nature structural & molecular biology 20090329 4
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 regula ...[more]