Serum and glucocorticoid-regulated kinase Sgk1 inhibits insulin-dependent activation of phosphomannomutase 2 in transfected COS-7 cells
作者： Miranda Menniti , Rodolfo Iuliano , Rosario Amato , Rosalia Boito , Monica Corea
DOI: 10.1152/AJPCELL.00284.2004
关键词: Glycoprotein 、 Phosphomannomutase 、 SGK1 、 Colocalization 、 Biochemistry 、 Kinase 、 Insulin 、 Glycosylation 、 Biology 、 Downregulation and upregulation
摘要: Serum- and glucocorticoid-regulated kinase (Sgk1) is considered to be an essential convergence point for peptide steroid regulation of ENaC-mediated sodium transport. We tried identify molecular partners Sgk1 by yeast two-hybrid screening. Yeast screening showed a specific interaction between phosphomannomutase (PMM)2, the latter which enzyme involved in glycoprotein biosynthesis. The was confirmed intact cells coimmunoprecipitation colocalization detected using confocal microscopy. were then able demonstrate that phosphorylated PMM2 vitro assay. In addition, we found enzymatic activity upregulated insulin treatment completely inhibits both absence presence stimulation. These data provide evidence suggesting may modulate action on cotranslational glycosylation glycoproteins.
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