Protein arginine methylation/demethylation and cancer
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Coralie Poulard1,2,3,4,5,6, Laura Corbo2,3,4,5,6 and Muriel Le Romancer2,3,4,5,6
1 Department of Biochemistry and Molecular Biology, University of Southern California Norris Comprehensive Cancer Center, University of Southern California Los Angeles, Los Angeles, CA, USA
2 Université de Lyon, Lyon, France
3 Université Lyon 1, Lyon, France
4 Inserm U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France
5 CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France
6 Equipe Labellisée, La Ligue Contre le Cancer, Paris, France
Muriel Le Romancer, email:
Keywords: PRMT, JMJD6, methylation, demethylation, cancer
Received: March 14, 2016 Accepted: August 09, 2016 Published: August 18, 2016
Protein arginine methylation is a common post-translational modification involved in numerous cellular processes including transcription, DNA repair, mRNA splicing and signal transduction. Currently, there are nine known members of the protein arginine methyltransferase (PRMT) family, but only one arginine demethylase has been identified, namely the Jumonji domain-containing 6 (JMJD6). Although its demethylase activity was initially challenged, its dual activity as an arginine demethylase and a lysine hydroxylase is now recognized. Interestingly, a growing number of substrates for arginine methylation and demethylation play key roles in tumorigenesis. Though alterations in the sequence of these enzymes have not been identified in cancer, their overexpression is associated with various cancers, suggesting that they could constitute targets for therapeutic strategies. In this review, we present the recent knowledge of the involvement of PRMTs and JMJD6 in tumorigenesis.
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