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Protein arginine methylation/demethylation and cancer

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 a...

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Detalles Bibliográficos
Autores principales: Poulard, Coralie, Corbo, Laura, Le Romancer, Muriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5341895/
https://www.ncbi.nlm.nih.gov/pubmed/27556302
http://dx.doi.org/10.18632/oncotarget.11376
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author Poulard, Coralie
Corbo, Laura
Le Romancer, Muriel
author_facet Poulard, Coralie
Corbo, Laura
Le Romancer, Muriel
author_sort Poulard, Coralie
collection PubMed
description 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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spelling pubmed-53418952017-03-23 Protein arginine methylation/demethylation and cancer Poulard, Coralie Corbo, Laura Le Romancer, Muriel Oncotarget Review 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. Impact Journals LLC 2016-08-18 /pmc/articles/PMC5341895/ /pubmed/27556302 http://dx.doi.org/10.18632/oncotarget.11376 Text en Copyright: © 2016 Poulard et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Review
Poulard, Coralie
Corbo, Laura
Le Romancer, Muriel
Protein arginine methylation/demethylation and cancer
title Protein arginine methylation/demethylation and cancer
title_full Protein arginine methylation/demethylation and cancer
title_fullStr Protein arginine methylation/demethylation and cancer
title_full_unstemmed Protein arginine methylation/demethylation and cancer
title_short Protein arginine methylation/demethylation and cancer
title_sort protein arginine methylation/demethylation and cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5341895/
https://www.ncbi.nlm.nih.gov/pubmed/27556302
http://dx.doi.org/10.18632/oncotarget.11376
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