Phosphorylation of LSD1 by PKC alpha Is Crucial for Circadian Rhythmicity and Phase Resetting
- Authors
- Nam, Hye Jin; Boo, Kyungjin; Kim, Dongha; Han, Dong-Hee; Choe, Han Kyoung; Kim, Chang Rok; Sun, Woong; Kim, Hyun; Kim, Kyungjin; Lee, Ho; Metzger, Eric; Schuele, Roland; Yoo, Seung-Hee; Takahashi, Joseph S.; Cho, Sehyung; Son, Gi Hoon; Baek, Sung Hee
- Issue Date
- 6-3월-2014
- Publisher
- CELL PRESS
- Citation
- MOLECULAR CELL, v.53, no.5, pp.791 - 805
- Indexed
- SCIE
SCOPUS
- Journal Title
- MOLECULAR CELL
- Volume
- 53
- Number
- 5
- Start Page
- 791
- End Page
- 805
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/99029
- DOI
- 10.1016/j.molcel.2014.01.028
- ISSN
- 1097-2765
- Abstract
- The circadian clock is a self-sustaining oscillator that controls daily rhythms. For the proper circadian gene expression, dynamic changes in chromatin structure are important. Although chromatin modifiers have been shown to play a role in circadian gene expression, the in vivo role of circadian signal-modulated chromatin modifiers at an organism level remains to be elucidated. Here, we provide evidence that the lysine-specific demethylase 1 (LSD1) is phosphorylated by protein kinase C alpha (PKC alpha) in a circadian manner and the phosphorylated LSD1 forms a complex with CLOCK:BMAL1 to facilitate E-box-mediated transcriptional activation. Knockin mice bearing phosphorylation-defective Lsd1(SA/SA) alleles exhibited altered circadian rhythms in locomotor behavior with attenuation of rhythmic expression of core clock genes and impaired phase resetting of circadian clock. These data demonstrate that LSD1 is a key component of the molecular circadian oscillator, which plays a pivotal role in rhythmicity and phase resetting of the circadian clock.
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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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