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首页> 外文期刊>Journal of Molecular Biochemistry >The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions
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The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions

机译：人糖皮质激素受体（hGR）的S-棕榈酸酯化在介导非基因组糖皮质激素作用中的作用

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Background: Many rapid nongenomic glucocorticoid actions are mediated by membrane-bound glucocorticoid receptors (GRs). S-palmitoylation is a lipid post-translational modification that mediates the membrane localization of some steroid receptors. A highly homologous amino acid sequence (663YLCM KTLLL671) is present in the ligand-binding domain of hGRα, suggesting that hGRα might also undergo S-palmitoylation. Aim: To investigate the role of the motif 663YLCMKTLLL671 in membrane localization of the hGRα and in mediating rapid nongenomic glucocorticoid signaling. Methods and Results: We showed that the mutant receptors hGRαY663A, hGRαC665A and hGRαLL670/671AA, and the addition of the palmitoylation inhibitor 2-bromopalmitate did not prevent membrane localization of hGRα and co-localization with caveolin-1, and did not influence the biphasic activation of mitogen-activated protein kinase (MAPK) signaling pathway in the early time points. Finally, the hGRα was not shown to undergo S-palmitoylation. Conclusions: The motif 663YLCMKTLLL671 does not play a role in membrane localization of hGRα and does not mediate the nongenomic glucocorticoid actions.
机译：背景：许多快速的非基因组糖皮质激素作用是由膜结合糖皮质激素受体（GRs）介导的。 S-棕榈酰化是脂质翻译后修饰，其介导某些类固醇受体的膜定位。 hGRα的配体结合域中存在高度同源的氨基酸序列（663YLCM KTLLL671），这表明hGRα也可能经历S-棕榈酰化。目的：研究基序663YLCMKTLLL671在hGRα的膜定位和介导快速非基因组糖皮质激素信号传导中的作用。方法和结果：我们表明，突变受体hGRαY663A，hGRαC665A和hGRαLL670/ 671AA，以及添加棕榈酰化抑制剂2-溴棕榈酸酯不会阻止hGRα的膜定位和与caveolin-1的共定位，并且不会影响双相在早期时间点激活丝裂原活化蛋白激酶（MAPK）信号通路。最后，未显示hGRα经历S-棕榈酰化。结论：基序663YLCMKTLLL671在hGRα的膜定位中不起作用，并且不介导非基因组糖皮质激素的作用。

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