Literature DB >> 20374708

Protein arginine methyltransferases: nuclear receptor coregulators and beyond.

Peter Kuhn1, Wei Xu.   

Abstract

Protein arginine methyltransferases (PRMTs) are a family of enzymes that play a crucial role in diverse cellular functions. Several PRMTs have been associated with gene expression regulation, in which PRMTs act as histone methyltransferases, secondary coregulators of transcription, or facilitate mRNA splicing and stability. Additional functions include modulation of protein localization, ribosomal assembly, and signal transduction. At the organismal level, several PRMTs appear to be important for development and may play an important role in cancer. The relationships between their cellular and organismal functions are poorly understood; at least in part due to the large body of enzymatic substrates for PRMTs and their transcriptional targets that remain to be determined. Specific PRMT inhibitors have been developed in recent years, which should help to shed light on their diverse biological roles. Connecting PRMT cellular functions with their global effects on an organism will facilitate development of novel treatments for human diseases.
Copyright © 2009 Elsevier Inc. All rights reserved.

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Year:  2009        PMID: 20374708     DOI: 10.1016/S1877-1173(09)87009-9

Source DB:  PubMed          Journal:  Prog Mol Biol Transl Sci        ISSN: 1877-1173            Impact factor:   3.622


  11 in total

1.  Histone H3R17me2a mark recruits human RNA polymerase-associated factor 1 complex to activate transcription.

Authors:  Jiacai Wu; Wei Xu
Journal:  Proc Natl Acad Sci U S A       Date:  2012-03-26       Impact factor: 11.205

Review 2.  Role of PRMTs in cancer: Could minor isoforms be leaving a mark?

Authors:  R Mitchell Baldwin; Alan Morettin; Jocelyn Côté
Journal:  World J Biol Chem       Date:  2014-05-26

3.  Expression and purification of full-length mouse CARM1 from transiently transfected HEK293T cells using HaloTag technology.

Authors:  Robert S Chumanov; Peter A Kuhn; Wei Xu; Richard R Burgess
Journal:  Protein Expr Purif       Date:  2010-11-30       Impact factor: 1.650

4.  PRMT5 dimethylates R30 of the p65 subunit to activate NF-κB.

Authors:  Han Wei; Benlian Wang; Masaru Miyagi; Yun She; Banu Gopalan; De-Bin Huang; Gourisankar Ghosh; George R Stark; Tao Lu
Journal:  Proc Natl Acad Sci U S A       Date:  2013-07-31       Impact factor: 11.205

Review 5.  Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.

Authors:  Nelmi O Devarie-Baez; Elsa I Silva Lopez; Cristina M Furdui
Journal:  Free Radic Res       Date:  2015-11-11

6.  Automethylation of CARM1 allows coupling of transcription and mRNA splicing.

Authors:  Peter Kuhn; Rob Chumanov; Yidan Wang; Ying Ge; Richard R Burgess; Wei Xu
Journal:  Nucleic Acids Res       Date:  2010-12-07       Impact factor: 16.971

7.  Differential CARM1 Isoform Expression in Subcellular Compartments and among Malignant and Benign Breast Tumors.

Authors:  David Shlensky; Jennifer A Mirrielees; Zibo Zhao; Lu Wang; Aparna Mahajan; Menggang Yu; Nathan M Sherer; Lee G Wilke; Wei Xu
Journal:  PLoS One       Date:  2015-06-01       Impact factor: 3.240

Review 8.  Roles of nitric oxide and asymmetric dimethylarginine in pregnancy and fetal programming.

Authors:  Li-Tung Huang; Chih-Sung Hsieh; Kow-Aung Chang; You-Lin Tain
Journal:  Int J Mol Sci       Date:  2012-11-09       Impact factor: 5.923

9.  CARM1 automethylation is controlled at the level of alternative splicing.

Authors:  Lu Wang; Purin Charoensuksai; Nikole J Watson; Xing Wang; Zibo Zhao; Carlos G Coriano; Leslie R Kerr; Wei Xu
Journal:  Nucleic Acids Res       Date:  2013-05-30       Impact factor: 16.971

Review 10.  Protein arginine methylation of non-histone proteins and its role in diseases.

Authors:  Han Wei; Rasika Mundade; Kevin C Lange; Tao Lu
Journal:  Cell Cycle       Date:  2013-12-02       Impact factor: 4.534

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