Protein arginine methylation of non-histone proteins and its role in diseases

Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on bo...

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Detalles Bibliográficos
Autores principales: Wei, Han, Mundade, Rasika, Lange, Kevin C, Lu, Tao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2014
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3925732/
https://www.ncbi.nlm.nih.gov/pubmed/24296620
http://dx.doi.org/10.4161/cc.27353
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author Wei, Han
Mundade, Rasika
Lange, Kevin C
Lu, Tao
author_facet Wei, Han
Mundade, Rasika
Lange, Kevin C
Lu, Tao
author_sort Wei, Han
collection PubMed
description Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs.
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spelling pubmed-39257322014-02-26 Protein arginine methylation of non-histone proteins and its role in diseases Wei, Han Mundade, Rasika Lange, Kevin C Lu, Tao Cell Cycle Review Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs. Landes Bioscience 2014-01-01 2013-12-02 /pmc/articles/PMC3925732/ /pubmed/24296620 http://dx.doi.org/10.4161/cc.27353 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Wei, Han
Mundade, Rasika
Lange, Kevin C
Lu, Tao
Protein arginine methylation of non-histone proteins and its role in diseases
title Protein arginine methylation of non-histone proteins and its role in diseases
title_full Protein arginine methylation of non-histone proteins and its role in diseases
title_fullStr Protein arginine methylation of non-histone proteins and its role in diseases
title_full_unstemmed Protein arginine methylation of non-histone proteins and its role in diseases
title_short Protein arginine methylation of non-histone proteins and its role in diseases
title_sort protein arginine methylation of non-histone proteins and its role in diseases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3925732/
https://www.ncbi.nlm.nih.gov/pubmed/24296620
http://dx.doi.org/10.4161/cc.27353
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