Unknown

Dataset Information

0

CK2alpha phosphorylates BMAL1 to regulate the mammalian clock.


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.

SUBMITTER: Tamaru T 

PROVIDER: S-EPMC6501789 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

CK2alpha phosphorylates BMAL1 to regulate the mammalian clock.

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]

Similar Datasets

| S-EPMC8648109 | biostudies-literature
| S-EPMC6343007 | biostudies-literature
| S-EPMC4642984 | biostudies-literature
| S-EPMC10182026 | biostudies-literature
| S-EPMC3756687 | biostudies-literature
| S-EPMC5771620 | biostudies-literature
2019-11-12 | PXD011721 | Pride
| S-EPMC2973897 | biostudies-other
| S-EPMC6347605 | biostudies-literature
| S-EPMC3404884 | biostudies-other