| First Author | Nam HJ | Year | 2014 |
| Journal | Mol Cell | Volume | 53 |
| Issue | 5 | Pages | 791-805 |
| PubMed ID | 24582500 | Mgi Jnum | J:210640 |
| Mgi Id | MGI:5571554 | Doi | 10.1016/j.molcel.2014.01.028 |
| Citation | Nam HJ, et al. (2014) Phosphorylation of LSD1 by PKCalpha is crucial for circadian rhythmicity and phase resetting. Mol Cell 53(5):791-805 |
| abstractText | 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 Calpha (PKCalpha) 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. |