Priority Research Papers:

SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells

Lianhua Piao, Takehiro Suzuki, Naoshi Dohmae, Yusuke Nakamura and Ryuji Hamamoto _

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Oncotarget. 2015; 6:16939-16950. https://doi.org/10.18632/oncotarget.4760

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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

Correspondence to:

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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PII: 4760