Journal
ONCOTARGET
Volume 6, Issue 19, Pages 16939-16950Publisher
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.4760
Keywords
SUV39H2; carcinogenesis; LSD1; non-histone protein methylation
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Funding
- NCATS NIH HHS [UL1 TR000430] Funding Source: Medline
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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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