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首页> 外文期刊>American Journal of Physiology >Serum and glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells.
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Serum and glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells.

机译：血清和糖皮质激素调节激酶Sgk1在转染的COS-7细胞中抑制胰岛素依赖性磷酸甘露糖突变酶2的活化。

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摘要

Serum- and glucocorticoid-regulated kinase (Sgk1) is considered to be an essential convergence point for peptide and steroid regulation of ENaC-mediated sodium transport. We tried to identify molecular partners of Sgk1 by yeast two-hybrid screening. Yeast two-hybrid screening showed a specific interaction between Sgk1 and phosphomannomutase (PMM)2, the latter of which is an enzyme involved in the regulation of glycoprotein biosynthesis. The interaction was confirmed in intact cells by coimmunoprecipitation and colocalization detected using confocal microscopy. We were then able to demonstrate that Sgk1 phosphorylated PMM2 in an in vitro assay. In addition, we found that the enzymatic activity of PMM2 is upregulated by insulin treatment and that Sgk1 completely inhibits PMM2 activity both in the absence and in the presence of insulin stimulation. These data provide evidence suggesting that Sgk1 may modulate insulin action on the cotranslational glycosylation of glycoproteins.
机译：血清和糖皮质激素调节激酶（Sgk1）被认为是肽和类固醇调节ENaC介导的钠转运的必不可少的收敛点。我们试图通过酵母双杂交筛选鉴定Sgk1的分子伴侣。酵母双杂交筛选显示Sgk1和磷酸甘露糖突变酶（PMM）2之间的特异性相互作用，后者是参与糖蛋白生物合成调控的酶。通过共免疫沉淀和共聚焦显微镜检测到的共定位，在完整细胞中证实了相互作用。然后，我们能够在体外分析中证明Sgk1磷酸化了PMM2。另外，我们发现，通过胰岛素治疗，PMM2的酶活性被上调，并且无论是否存在胰岛素刺激，Sgk1都会完全抑制PMM2的活性。这些数据提供的证据表明，Sgk1可能调节胰岛素对糖蛋白共翻译糖基化的作用。

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