Priority Research Papers:
SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells
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Lianhua Piao1, Takehiro Suzuki2, Naoshi Dohmae2, Yusuke Nakamura1 and Ryuji Hamamoto1
1 Section of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL, USA
2 Biomolecular Characterizaion Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama, Japan
Ryuji Hamamoto, email:
Keywords: SUV39H2, carcinogenesis, LSD1, non-histone protein methylation
Received: May 02, 2015 Accepted: June 26, 2015 Published: July 03, 2015
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.
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