Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation.
作者： Nathalie Filippa , Carol L. Sable , Brian A. Hemmings , Emmanuel Van Obberghen
DOI: 10.1128/MCB.20.15.5712-5721.2000
关键词:
摘要: In this report we investigated the function of phosphoinositide-dependent protein kinase 1 (PDK1) in B (PKB) activation and translocation to cell surface. Wild-type PDK1 mutants were transfected into HeLa cells, their subcellular localization was analyzed. found translocate plasma membrane response insulin, process did not require a functional catalytic activity, since catalytically inactive mutant (Kd) capable translocating. The presence at surface shown be linked phospholipids therefore serum-dependent phosphatidylinositol 3-kinase activity. Using confocal microscopy cells that colocalizes with PKB membrane. Further, after cotransfection (Mut) unable membrane, prevented from moving periphery insulin stimulation. its PH domain deleted (ΔPH-PKB) retained ability when coexpressed PDK1. Finally, ΔPH-PKB highly active independent stimulation cotransfected defective domain. These findings suggest brings upon exposure acts as negative regulator enzyme
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