Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex.
Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex.
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DOI：
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发表时间：
2005
影响因子：
21.3
通讯作者：
A. Hausser;P. Storz;S. Märtens;G. Link;A. Toker;K. Pfizenmaier
中科院分区：
文献类型：
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作者：
A. Hausser;P. Storz;S. Märtens;G. Link;A. Toker;K. Pfizenmaier
蛋白激酶D(PKD)调节来源于反高尔基体网的囊泡的分裂。我们发现磷脂酰肌醇4-激酶IIIbeta(PI4KIIIbeta)--高尔基复合体结构和功能中的一个关键角色--是PKD的生理底物。在三种PKD亚型中，只有PKD1和PKD2在从酵母到人类高度保守的基序上磷酸化PI4KIIIbeta。PKD介导的磷酸化刺激了PI4KIIIbeta的脂激酶活性，并促进了水泡性口炎病毒G蛋白向质膜的转运。PI4KIIIbeta作为PKD底物之一的鉴定应该有助于揭示使运输载体形成的分子事件。
Protein kinase D (PKD) regulates the fission of vesicles originating from the trans-Golgi network. We show that phosphatidylinositol 4-kinase IIIbeta (PI4KIIIbeta) - a key player in the structure and function of the Golgi complex - is a physiological substrate of PKD. Of the three PKD isoforms, only PKD1 and PKD2 phosphorylated PI4KIIIbeta at a motif that is highly conserved from yeast to humans. PKD-mediated phosphorylation stimulated lipid kinase activity of PI4KIIIbeta and enhanced vesicular stomatitis virus G-protein transport to the plasma membrane. The identification of PI4KIIIbeta as one of the PKD substrates should help to reveal the molecular events that enable transport-carrier formation.