Phosphorylation of PPARs:: from molecular characterization to physiological relevance
Phosphorylation of PPARs:: from molecular characterization to physiological relevance
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DOI：
10.1016/j.biochi.2004.11.010
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发表时间：
2005-01-01
期刊：
影响因子：
3.9
通讯作者：
Pégorier, JP
中科院分区：
文献类型：
--
作者：
Diradourian, C;Girard, J;Pégorier, JP
除了配体介导的激活外，核受体的活性还受到它们的磷酸化状态的微调。PPAR被几种激酶(PKA、PKC、MAPKs和AMPK)磷酸化，根据异构体和细胞环境的不同，它们以配体依赖或非配体依赖的方式影响其活性。分子后果是多方面的，包括配体亲和力的变化，DNA结合，转录辅助因子的招募，蛋白酶体降解…最后，讨论了PPAR磷酸化的生理相关性。(C)2004年爱思唯尔公司。版权所有。
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.