SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells
By Lianhua Piao, Takehiro Suzuki, N. Dohmae, Yusuke Nakamura, Ryuji Hamamoto. 2015
50 citations recorded by the source corpus.
LSD1 is a histone lysine demethylase, which is highly expressed in multiple types of human cancer. Although its roles in transcriptional regulation have been well-studied, functional regulation of LSD1 by post-translational modifications still remains unknown. Here, we demonstrate that the histone lysine methyltransferase SUV39H2 trimethylated LSD1 on lysine 322. Knockdown of SUV39H2 resulted in a decrease of LSD1 protein even though the mRNA levels were unchanged. SUV39H2-induced LSD1 methylation suppresses LSD1 polyubiquitination and subsequent degradation. In addition, we also observed indirect effect of SUV39H2 overexpression on LSD1-target genes. Our results reveal the regulatory mechanism of LSD1 protein through its lysine methylation by SUV39H2 in human cancer cells.
Subfields: Molecular Biology
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In Molecular Biology
- Ryuji Hamamoto
- Yusuke Nakamura
- N. Dohmae
- Takehiro Suzuki
- Makoto Nakakido
- Lianhua Piao
- Yuichiro Yoshioka
- S. Hayami
Citations in the corpus
- PRMT1 promotes mitosis of cancer cells through arginine methylation of INCENP (2015, methodology): “In vitro methyltransferase assays were described previously [37, 39-46].”
- Deregulation of the Histone Lysine-Specific Demethylase 1 Is Involved in Human Hepatocellular Carcinoma (2019, background): “These epigenetic changes caused by LSD1 have been shown to play a key role in human tumorigenesis [18,25,47].”
- SMYD3-mediated lysine methylation in the PH domain is critical for activation of AKT1 (2016, unknown): “8, 10 mM dithiothreitol (DTT) and 10 mM MgCl 2 ), for 2 hours at 30°C [37–46].”