Journal
MOLECULAR CELL
Volume 53, Issue 5, Pages 791-805Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2014.01.028
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Funding
- Creative Research Initiatives Program (Research Center for Chromatin Dynamics) [2009-0081563]
- Korea Research Foundation (KRF) [2009-0088886]
- ICT and Future Planning Program [2012049932]
- DFG [Schu688/9-1, Schu688/10-2, Schu688/11-2, Schu688/12-1]
- ERC [322844-LSD1]
- National Research Foundation (NRF)
- Korea government (MSIP)
- National Research Foundation of Korea [2009-0088886] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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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