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首页> 外文期刊>Advances in enzyme regulation >Protein phosphatase regulation by PRIP, a PLC-related catalytically inactive protein--implications in the phospho-modulation of the GABAA receptor.
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Protein phosphatase regulation by PRIP, a PLC-related catalytically inactive protein--implications in the phospho-modulation of the GABAA receptor.

机译：PRIP是一种与PLC相关的催化失活蛋白，通过PRIP调节蛋白磷酸酶-暗示GABAA受体的磷酸调节。

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摘要

PRIP, phospholipase C related, but catalytically inactive protein was first identified as a novel inositol 1,4,5-trisphosphate binding protein. It has a number of binding partners including protein phosphatase (PP1 and 2A), GABAA receptor associated protein, and the beta subunits of GABAA receptors, in addition to inositol 1,4,5-trisphosphate. The identification of these molecules led us to examine the possible involvement of PRIP in the phospho-regulation of the beta subunits of GABAA receptors using hippocampal neurons prepared from PRIP-1 and 2 double knock-out (DKO) mice. Experiments were performed with special reference to the dephosphorylation processes of the beta subunits. The phosphorylation of beta3 subunits by the activation of protein kinase A in cortical neurons of the control mice continued for up to 5 min, even after washing out of the stimulus, followed by a gradual dephosphorylation. That of DKO mice gradually increased in spite of the lower phosphorylation levels induced by the stimulation. There was little difference in the amount of cellular cyclic AMP and protein kinase A activity between the control and mutant mice, indicating that phosphatases such as PP1 and PP2A are primarily involved in the difference. The time course of PP1 activity changes in the vicinity of the receptors in control mice corresponded to the phosphorylation of PRIP, while that of the mutant mice decreased with the period of the incubation. This is a good agreement with the suggestion that PRIP binds to and inactivates PP1, which is regulated by the phosphorylation of PRIP at threonine 94. These results suggest that PRIP plays an important role in controlling the dynamics of GABAA receptor phosphorylation by through PP1 binding and, therefore, the efficacy of synaptic inhibition mediated by these receptors.
机译：PRIP，磷脂酶C相关，但催化失活的蛋白质首先被鉴定为新型的肌醇1,4,5-三磷酸结合蛋白。除肌醇1,4,5-三磷酸酯外，它还具有许多结合伴侣，包括蛋白磷酸酶（PP1和2A），GABAA受体相关蛋白和GABAA受体的β亚基。这些分子的鉴定使我们使用从PRIP-1和2双敲除（DKO）小鼠制备的海马神经元来检查PRIP可能参与GABAA受体的β亚基的磷酸调节。进行的实验特别参考了β亚基的去磷酸化过程。即使在刺激物洗掉后，由对照小鼠的皮质神经元中的蛋白激酶A激活，β3亚基的磷酸化仍持续长达5分钟，然后逐渐进行去磷酸化。尽管刺激引起的磷酸化水平较低，但DKO小鼠的体重逐渐升高。对照小鼠和突变小鼠之间细胞环AMP和蛋白激酶A活性的量几乎没有差异，表明磷酸酶（例如PP1和PP2A）主要参与了差异。对照小鼠中受体附近PP1活性的时间变化与PRIP的磷酸化相对应，而突变小鼠的PP1活性随培养时间的延长而降低。这与PRIP结合并灭活PP1有关，这是受苏氨酸94上的PRIP磷酸化调节的。这是一个很好的建议。这些结果表明PRIP通过PP1的结合和在控制GABAA受体磷酸化的动力学中起着重要作用。因此，这些受体介导的突触抑制的功效。

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