Phosphorylation of PPARs:: from molecular characterization to physiological relevance

被引：144

作者：

Diradourian, C ^{[1
]}

Girard, J ^{[1
]}

Pégorier, JP ^{[1
]}

机构：

[1] Univ Paris 05, CNRS, Inst Cochin, INSERM,U567,UMR8104,Dept Endocrinol, F-75014 Paris, France

来源：

BIOCHIMIE | 2005年 / 87卷 / 01期

关键词：

PPAR; transcriptional activity; phosphorylation and kinases;

D O I：

10.1016/j.biochi.2004.11.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In addition to their ligand-mediated activation, nuclear receptor activity is finely tuned by their phosphorylation status. PPARs are phosphorylated by several kinases (PKA, PKC, MAPKs, and AMPK), which affect their activity in a ligand-dependent or -independent manner according to the isoform and cellular context. Molecular consequences are multiple, including changes in ligand affinity, DNA binding, recruitment of transcriptional cofactors, proteasome degradation... Finally, the physiological relevance of PPAR phosphorylation is discussed. (c) 2004 Elsevier SAS. All rights reserved.

引用

页码：33 / 38

页数：6

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