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Dimerization of cGMP-dependent protein kinase 1 alpha and the myosin-binding subunit of myosin phosphatase: role of leucine zipper domains

机译：cGMP依赖性蛋白激酶1α和肌球蛋白磷酸酶的肌球蛋白结合亚基的二聚：亮氨酸拉链域的作用。

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Nitric oxide (NO) and nitrovasodilators induce vascular smooth muscle cell relaxation in part by cGMP-dependent protein kinase (cGK)mediated activation of myosin phosphatase, which dephosphorylates myosin light chains. We recently found that cGMP-dependent protein kinase 1alpha binds directly to the myosin-binding subunit (NIBS) of myosin phosphatase via the leucine/isoleucine zipper of cGK. We have now studied the role of the leucine zipper domain of MBS in dimerization with cGK and the leucine/isoleucine zipper and leucine zipper domains of both proteins in homodimerization. Mutagenesis of the NIBS leucine zipper domain disrupts cGKIalpha-MBS dimerization. Mutagenesis of the MBS leucine zipper eliminates NIBS homodimerization, while similar disruption of the cGKIalpha leucine/isoleucine zipper does not prevent formation of cGK dimers. The MBS leucine zipper domain is phosphorylated by cGK, but this does not have any apparent effect on heterodimer formation between the two proteins. MBS LZ mutants that are unable to bind cGK were poor substrates for cGK. These data support the theory that the MBS leucine zipper domain is necessary and sufficient to mediate both NIBS homodinterization and binding of the protein to cGK. In contrast, the leucine/isoleucine zipper of cGK is required for binding to MBS, but not for cGK homodimerization. These data support that the MBS and cGK leucine zipper domains mediate the interaction between these two proteins. The contribution of these domains to both homodimerization and their specific interaction with each other suggest that additional regulatory mechanisms involving these domains may exist. (C) 2003 Published by Elsevier Science Inc. [References: 41]
机译：一氧化氮（NO）和硝化血管舒张剂部分地由cGMP依赖性蛋白激酶（cGK）介导的肌球蛋白磷酸酶激活引起血管平滑肌细胞松弛，从而使肌球蛋白轻链脱磷酸。我们最近发现cGMP依赖性蛋白激酶1α通过cGK的亮氨酸/异亮氨酸拉链直接与肌球蛋白磷酸酶的肌球蛋白结合亚基（NIBS）结合。现在，我们已经研究了MBS的亮氨酸拉链结构域在与cGK二聚化中的作用，以及在同型二聚化中两种蛋白的亮氨酸/异亮氨酸拉链和亮氨酸拉链结构域中的作用。 NIBS亮氨酸拉链结构域的诱变会破坏cGKIalpha-MBS二聚化。 MBS亮氨酸拉链的诱变消除了NIBS的二聚化作用，而cGKIalpha亮氨酸/异亮氨酸拉链的类似破坏并不能阻止cGK二聚体的形成。 MBS亮氨酸拉链结构域被cGK磷酸化，但这对这两种蛋白之间的异二聚体形成没有明显影响。无法结合cGK的MBS LZ突变体是cGK的底物。这些数据支持以下理论：MBS亮氨酸拉链结构域对于介导NIBS均质化和蛋白质与cGK的结合都是必需和充分的。相反，cGK的亮氨酸/异亮氨酸拉链与MBS结合是必需的，但cGK均二聚化则不需要。这些数据支持MBS和cGK亮氨酸拉链结构域介导这两种蛋白之间的相互作用。这些结构域对均二聚化及其相互之间的特异性相互作用的贡献表明，可能存在涉及这些结构域的其他调控机制。 （C）2003年由Elsevier Science Inc.出版。[参考：41]

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