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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Phosphorylation and activation of PINOID by the phospholipid signaling kinase 3-phosphoinositidedependent protein kinase 1 (PDK1) in Arabidopsis
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Phosphorylation and activation of PINOID by the phospholipid signaling kinase 3-phosphoinositidedependent protein kinase 1 (PDK1) in Arabidopsis

机译：拟南芥中磷脂信号激酶3-磷酸肌醇依赖性蛋白激酶1（PDK1）对PINOID的磷酸化和激活

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摘要

Activity of the serine-threonine protein kinase PINOID (PID) has been implicated in the asymmetrical localization of the membrane-associated PINFORMED (PIN) family of auxin transport facilitators. However, the means by which PID regulates PIN protein distribution is unknown. We have used recombinant PID protein to dissect the regulation of PID activity in vitro. We demonstrate that intramolecular PID autophosphorylation is required for the ability of PID to phosphorylate an exogenous substrate. PID-like mammalian AGC kinases act in a phosphorylation cascade initiated by the phospholipid-associated kinase, 3-phosphoinositide-dependent protein kinase 1 (PDK1), which binds to the C-terminal hydrophobic PDK1-interacting fragment (PIF) domain found in PDK1 substrates. We find that Arabidopsis PDK1 interacts with PID, and that transphosphorylation by PDK1 increases PID autophosphorylation. We show that a PID activation loop serine is required for PDK1-dependent PID phosphorylation. This activation is rapid and requires the PIF domain. Cell extracts from flowers and seedling shoots dramatically increase PID phosphorylation in a tissue-specific manner. A PID protein variant in which the PIF domain was mutated failed to be activated by the seedling shoot extracts. PID immunoprecipitated from Arabidopsis cells in which PDK1 expression was inhibited by RNAi showed a dramatic reduction in transphosphorylation of myelin basic protein substrate. These results indicate that AtPDK1 is a potent enhancer of PID activity and provide evidence that phospholipid signaling may play a role in the signaling processes controlling polar auxin transport.
机译：丝氨酸-苏氨酸蛋白激酶PINOID（PID）的活性与生长素运输促进剂的膜相关PINFORMED（PIN）家族的不对称定位有关。但是，PID调节PIN蛋白分布的方法尚不清楚。我们已经使用重组PID蛋白来解剖PID活性的体外调节。我们证明分子内PID自磷酸化是PID磷酸化外源底物的能力所必需的。 PID样哺乳动物AGC激酶在磷脂相关激酶3-磷酸肌醇依赖性蛋白激酶1（PDK1）引发的磷酸化级联反应中起作用，该激酶与PDK1中的C端疏水性PDK1相互作用片段（PIF）域结合基材。我们发现拟南芥PDK1与PID相互作用，并且PDK1的转磷酸化增加了PID的自磷酸化。我们显示，PDK1依赖的PID磷酸化需要PID激活环丝氨酸。此激活速度很快，并且需要PIF域。从花和幼苗的芽中提取的细胞以组织特异性的方式显着增加了PID的磷酸化。 PIF结构域发生突变的PID蛋白变体未能被苗芽提取物激活。从拟南芥细胞中免疫沉淀的PID被RNAi抑制了PDK1的表达，表明髓磷脂碱性蛋白底物的转磷酸作用显着降低。这些结果表明AtPDK1是PID活性的有效增强剂，并提供了磷脂信号传导可能在控制极性植物生长素转运的信号传导过程中起作用的证据。

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