Protein arginine methylation in estrogen signaling and estrogen-related cancers

被引:34
|
作者
Teyssier, Catherine [5 ,6 ,7 ]
Le Romancer, Muriel [8 ,9 ,10 ]
Sentis, Stephanie [8 ,9 ,10 ]
Jalaguier, Stephan [1 ,2 ,3 ,4 ]
Corbo, Laura [8 ,9 ,10 ]
Cavailles, Vincent [1 ,2 ,3 ,4 ]
机构
[1] IRCM, F-34298 Montpellier, France
[2] INSERM, U896, F-34298 Montpellier, France
[3] Univ Montpellier 1, F-34298 Montpellier, France
[4] Ctr Val dAurelle Paul Lamarque CRLC, F-34298 Montpellier, France
[5] INSERM, U554, F-34090 Montpellier, France
[6] Univ Montpellier 1, CNRS, UMR5048, Ctr Biochim Struct, F-34090 Montpellier, France
[7] Univ Montpellier 2, F-34090 Montpellier, France
[8] Univ Lyon 1, INSERM, U590, Equipe Labellisee La Ligue,ISPB, F-69003 Lyon, France
[9] IFR62, F-69003 Lyon, France
[10] Ctr Leon Berard, F-69008 Lyon, France
来源
关键词
RECEPTOR COACTIVATOR AIB1; HUMAN BREAST-CANCER; TRANSCRIPTIONAL REGULATION; METHYLTRANSFERASE CARM1; HISTONE MODIFICATIONS; EXPRESSION SIGNATURE; N-METHYLTRANSFERASE; LYSINE METHYLATION; PADI4; EXPRESSION; GENE;
D O I
10.1016/j.tem.2009.11.002
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Estrogen signaling pathways regulate multiple cellular processes including proliferation and differentiation, and dysregulation of these pathways underlies several human pathologies. Post-translational modifications (PTMs) play an important role in estrogen signaling. This review focuses on recent findings pertinent to arginine methylation of non-histone proteins and their implications in estrogen signaling. We describe protein arginine methyltransferases and demethylases, the role of methylarginine proteins in estrogen action and crosstalk with other PTMs such as phosphorylation and lysine methylation. The relationships between various PTMs form a specific code that is likely to play an important role in hormone signaling. In addition, dysregulation of arginine methylation or of enzymes responsible for these modifications could be key events in estrogen-dependent cancers such as breast cancer.
引用
收藏
页码:181 / 189
页数:9
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