The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation

Lan Wang, Alexander Gural, Xiao Jian Sun, Xinyang Zhao, Fabiana Perna, Gang Huang, Megan A. Hatlen, Ly Vu, Fan Liu, Haiming Xu, Takashi Asai, Hao Xu, Tony Deblasio, Silvia Menendez, Francesca Voza, Yanwen Jiang, Philip A. Cole, Jinsong Zhang, Ari Melnick, Robert G. RoederStephen D. Nimer

Research output: Contribution to journalArticlepeer-review

165 Scopus citations


The chromosomal translocations found in acute myelogenous leukemia (AML) generate oncogenic fusion transcription factors with aberrant transcriptional regulatory properties. Although therapeutic targeting of most leukemia fusion proteins remains elusive, the posttranslational modifications that control their function could be targetable. We found that AML1-ETO, the fusion protein generated by the t(8;21) translocation, is acetylated by the transcriptional coactivator p300 in leukemia cells isolated from t(8;21) AML patients, and that this acetylation is essential for its self-renewal-promoting effects in human cord blood CD34+ cells and its leukemogenicity in mouse models. Inhibition of p300 abrogates the acetylation of AML1-ETO and impairs its ability to promote leukemic transformation. Thus, lysine acetyltransferases represent a potential therapeutic target in AML.

Original languageEnglish (US)
Pages (from-to)765-769
Number of pages5
Issue number6043
StatePublished - Aug 5 2011
Externally publishedYes

ASJC Scopus subject areas

  • General


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