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首页> 外文期刊>Advances in biological regulation >Phospholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation
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Phospholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation

机译：磷脂酶C相关但无催化活性的蛋白PRIP作为磷酸调节的支架蛋白

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摘要

PRIP, phospholipase C (PLC)-related but catalytically inactive protein is a protein with a domain organization similar to PLC-δ1. We have reported that PRIP interacts with the catalytic subunits of protein phosphatase 1 and 2A (PP1c and PP2Ac), depending on the phosphorylation of PRIP. We also found that Akt was precipitated along with PRIP by anti-PRIP antibody from neuronal cells. In this article, we summarize our current reach regarding the interaction of PRIP with Akt and protein phosphatases, in relation to the cellular phospho-regulations. PP1 and PP2A are major members of the protein serine/threonine phosphatase families. We have identified PP1 and PP2A as interacting partners of PRIP. We first investigated the interaction of PRIP with two phosphatases, using purified recombinant proteins. PRIP immobilized on beads pulled-down the catalytic subunits of both PP1 and PP2A, indicating that the interactions were in a direct manner, and the binding of PP1 and PP2A to PRIP were mutually exclusive. Site-directed mutagenesis experiments revealed that the binding sites for PP1 and PP2A on PRIP were not identical, but in close proximity. Phosphorylation of PRIP by protein kinase A (PKA) resulted in the reduced binding of PP1, but not PP2A. Rather, the dissociation of PP1 from PRIP by phosphorylation accompanied the increased binding of PP2A in invitro experiments. This binding regulation of PP1 and PP2A to PRIP by PKA-dependent phosphorylation was also observed in living cells treated with forskolin or isoproterenol. These results suggested that PRIP directly interacts with the catalytic subunits of two distinct phosphatases in a mutually exclusive manner and the interactions are regulated by phosphorylation, thus functioning as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling.
机译：PRIP，磷脂酶C（PLC）相关但催化失活的蛋白质，是一种结构域类似于PLC-δ1的蛋白质。我们已经报告说PRIP与蛋白质磷酸酶1和2A的催化亚基（PP1c和PP2Ac）相互作用，这取决于PRIP的磷酸化作用。我们还发现Akt与PRIP一起通过抗PRIP抗体从神经元细胞中沉淀出来。在本文中，我们总结了目前有关PRIP与Akt和蛋白质磷酸酶相互作用的影响，以及与细胞磷酸调节有关的影响。 PP1和PP2A是蛋白质丝氨酸/苏氨酸磷酸酶家族的主要成员。我们已将PP1和PP2A确定为PRIP的交互伙伴。我们首先使用纯化的重组蛋白研究了PRIP与两种磷酸酶的相互作用。 PRIP固定在珠子上，使PP1和PP2A的催化亚基均被拉下，表明相互作用是直接的，并且PP1和PP2A与PRIP的结合是互斥的。定点诱变实验表明，PRIP上PP1和PP2A的结合位点不完全相同，但很接近。蛋白激酶A（PKA）使PRIP磷酸化导致PP1结合力降低，但PP2A结合力降低。相反，在体外实验中，PP1通过磷酸化从PRIP上解离伴随着PP2A结合的增加。在用毛喉素或异丙肾上腺素处理的活细胞中也观察到PKA和PP2A通过PRA依赖性磷酸化与PRIP的这种结合调节。这些结果表明PRIP以相互排斥的方式直接与两个不同磷酸酶的催化​​亚基相互作用，并且相互作用通过磷酸化来调节，因此起着调节磷酸依赖性细胞中PP1和PP2A的活性和亚细胞定位的支架的作用。信号。

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