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首页> 外文期刊>The Journal of biological chemistry >Peptidyl-prolyl Isomerase Pin1 Controls Down-regulation of Conventional Protein Kinase C Isozymes
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Peptidyl-prolyl Isomerase Pin1 Controls Down-regulation of Conventional Protein Kinase C Isozymes

机译：肽基 - 脯氨酰异构酶PIN1控制常规蛋白激酶C同工酶的下调

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摘要

The down-regulation or cellular depletion of protein kinase C (PKC) attendant to prolonged activation by phorbol esters is a widely described property of this key family of signaling enzymes. However, neither the mechanism of down-regulation nor whether this mechanism occurs following stimulation by physiological agonists is known. Here we show that the peptidyl-prolyl isomerase Pin1 provides a timer for the lifetime of conventional PKC isozymes, converting the enzymes into a species that can be dephosphorylated and ubiquitinated following activation induced by either phorbol esters or natural agonists. The regulation by Pin1 requires both the catalytic activity of the isomerase and the presence of a Pro immediately following the phosphorylated Thr of the turn motif phosphorylation site, one of two C-terminal sites that is phosphorylated during the maturation of PKC isozymes. Furthermore, the second C-terminal phosphorylation site, the hydrophobic motif, docks Pin1 to PKC. Our data are consistent with a model in which Pin1 binds the hydrophobic motif of conventional PKC isozymes to catalyze the isomerization of the phospho-Thr-Pro peptide bond at the turn motif, thus converting these PKC isozymes into species that can be efficiently down-regulated following activation.
机译：蛋白激酶C（PKC）伴者通过Phorbol酯长期活化的蛋白激酶C（PKC）耗尽是该关键信号传导酶的广泛描述的性质。然而，未知，下调的机制也不是通过生理激动剂刺激发生这种机制。在这里，我们表明肽基 - 脯氨酰异构酶PIN1为常规PKC同工酶的寿命提供定时器，将酶转化为可以在磷酸酯或天然激动剂诱导的激活后可以去磷酸化和泛染的物种。 PIN1的调节需要异构酶的催化活性和在转动基序磷酸化位点的磷酸化TH之后，在PKC同工酶的成熟期间磷酸化的两个C末端位点之一后立即存在Pro的存在。此外，第二个C末端磷酸化位点，疏水基序，码头PIN1至PKC。我们的数据与PIN1结合常规PKC同工酶的疏水基序的模型一致，以催化转弯基序的磷酸基-PRO肽键的异构化，从而将这些PKC同工酶转化为可以有效地下调的物种激活后。

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