Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase

PRMT2 belongs to the protein arginine methyltransferase (PRMT) family, which catalyzes the arginine methylation of target proteins. As a type I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to have weak methyltransferase activity on histone substrates in vitro, suggesting th...

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Autores principales:	Vincent Cura, Jean Cavarelli
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	protein arginine methylation PRMT2 epigenetics SH3 cancer Science Q
Acceso en línea:	https://doaj.org/article/a1c00adca2f646d2b7a4825e34f20b59
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spelling	oai:doaj.org-article:a1c00adca2f646d2b7a4825e34f20b592021-11-25T18:11:40ZStructure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase10.3390/life111112632075-1729https://doaj.org/article/a1c00adca2f646d2b7a4825e34f20b592021-11-01T00:00:00Zhttps://www.mdpi.com/2075-1729/11/11/1263https://doaj.org/toc/2075-1729PRMT2 belongs to the protein arginine methyltransferase (PRMT) family, which catalyzes the arginine methylation of target proteins. As a type I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to have weak methyltransferase activity on histone substrates in vitro, suggesting that its authentic substrates have not yet been found. PRMT2 contains the canonical PRMT methylation core and a unique Src homology 3 domain. Studies have demonstrated its clear implication in many different cellular processes. PRMT2 acts as a coactivator of several nuclear hormone receptors and is known to interact with a multitude of splicing-related proteins. Furthermore, PRMT2 is aberrantly expressed in several cancer types, including breast cancer and glioblastoma. These reports highlight the crucial role played by PRMT2 and the need for a better characterization of its activity and cellular functions.Vincent CuraJean CavarelliMDPI AGarticleprotein arginine methylationPRMT2epigeneticsSH3cancerScienceQENLife, Vol 11, Iss 1263, p 1263 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	protein arginine methylation PRMT2 epigenetics SH3 cancer Science Q
spellingShingle	protein arginine methylation PRMT2 epigenetics SH3 cancer Science Q Vincent Cura Jean Cavarelli Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
description	PRMT2 belongs to the protein arginine methyltransferase (PRMT) family, which catalyzes the arginine methylation of target proteins. As a type I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to have weak methyltransferase activity on histone substrates in vitro, suggesting that its authentic substrates have not yet been found. PRMT2 contains the canonical PRMT methylation core and a unique Src homology 3 domain. Studies have demonstrated its clear implication in many different cellular processes. PRMT2 acts as a coactivator of several nuclear hormone receptors and is known to interact with a multitude of splicing-related proteins. Furthermore, PRMT2 is aberrantly expressed in several cancer types, including breast cancer and glioblastoma. These reports highlight the crucial role played by PRMT2 and the need for a better characterization of its activity and cellular functions.
format	article
author	Vincent Cura Jean Cavarelli
author_facet	Vincent Cura Jean Cavarelli
author_sort	Vincent Cura
title	Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
title_short	Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
title_full	Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
title_fullStr	Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
title_full_unstemmed	Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase
title_sort	structure, activity and function of the prmt2 protein arginine methyltransferase
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/a1c00adca2f646d2b7a4825e34f20b59
work_keys_str_mv	AT vincentcura structureactivityandfunctionoftheprmt2proteinargininemethyltransferase AT jeancavarelli structureactivityandfunctionoftheprmt2proteinargininemethyltransferase
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Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase

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