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Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Semi-quantitative mass spectrometry in AML cells identifies new non-genomic targets of the EZH2 methyltransferase
Author(s): Sbirkov, Yordan
Kwok, Colin
Bhamra, Amandeep
Thompson, Andrew J
Gil, Veronica
Zelent, Arthur
Petrie, Kevin
Keywords: acute myeloid leukaemia
mass spectrometry
Issue Date: 5-Jul-2017
Citation: Sbirkov Y, Kwok C, Bhamra A, Thompson AJ, Gil V, Zelent A & Petrie K (2017) Semi-quantitative mass spectrometry in AML cells identifies new non-genomic targets of the EZH2 methyltransferase, International Journal of Molecular Sciences, 18 (7), Art. No.: 1440.
Abstract: Alterations to the gene encoding the EZH2 (KMT6A) methyltransferase, including both gain-of-function and loss-of-function, have been linked to a variety of haematological malignancies and solid tumours, suggesting a complex, context-dependent role of this methyltransferase. The successful implementation of molecularly targeted therapies against EZH2 requires a greater understanding of the potential mechanisms by which EZH2 contributes to cancer. One aspect of this effort is the mapping of EZH2 partner proteins and cellular targets. To this end we performed affinity-purification mass spectrometry in the FAB-M2 HL-60 acute myeloid leukaemia (AML) cell line before and after all-transretinoic acid-induced differentiation. These studies identified new EZH2 interaction partners and potential non-histone substrates for EZH2-mediated methylation. Our results suggest that EZH2 is involved in the regulation of translation through interactions with a number of RNA binding proteins and by methylating key components of protein synthesis such as eEF1A1. Given that deregulated mRNA translation is a frequent feature of cancer and that eEF1A1 is highly expressed in many human tumours, these findings present new possibilities for the therapeutic targeting of EZH2 in AML.
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Rights: © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (

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