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SUV39H2 Methylates and Stabilizes LSD1 by Inhibiting Polyubiquitination in Human Cancer Cells

SUV39H2 Methylates and Stabilizes LSD1 by Inhibiting Polyubiquitination in Human Cancer Cells

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

Oncotarget. 2015 Jul 10;6(19):16939-50.

PMID: 26183527

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416095	SUV39H2 human			Price

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