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首页> 外文期刊>Molecular biology of the cell >Nuclear export and plasma membrane recruitment of the Ste5 scaffold are coordinated with oligomerization and association with signal transduction components
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Nuclear export and plasma membrane recruitment of the Ste5 scaffold are coordinated with oligomerization and association with signal transduction components

机译：Ste5支架的核输出和质膜募集与寡聚化以及与信号转导成分的结合相协调

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摘要

The Ste5 scaffold activates an associated mitogen-activated protein kinase cascade by binding through its RING-H2 domain to a Gbetagamma dimer (Ste4/Ste18) at the plasma membrane in a recruitment event that requires prior nuclear shuttling of Ste5. Genetic evidence suggests that Ste5 must oligomerize to function, but its impact on Ste5 function and localization is unknown. Herein, we show that oligomerization affects Ste5 activity and localization. The majority of Ste5 is monomeric, suggesting that oligomerization is tightly regulated. Increasing the pool of Ste5 oligomers increases association with Ste11. Remarkably, Ste5 oligomers are also more efficiently exported from the nucleus, retained in the cytoplasm by Ste11 and better recruited to the plasma membrane, resulting in constitutive activation of the mating mitogen-activated protein kinase cascade. Co-precipitation tests show that the RING-H2 domain is the key determinant of oligomerization. Mutational analysis suggests that the leucine-rich domain limits the accessibility of the RING-H2 domain and inhibits export and recruitment in addition to promoting Ste11 association and activation. Our results suggest that the major form of Ste5 is an inactive monomer with an inaccessible RING-H2 domain and Ste11 binding site, whereas the active form is an oligomer that is more efficiently exported and recruited and has a more accessible RING-H2 domain and Ste11 binding site. [References: 46]
机译：在需要事先对Ste5进行核穿梭的募集事件中，Ste5支架通过其RING-H2域与质膜上的Gbetagamma二聚体（Ste4 / Ste18）结合，从而激活相关的促丝裂原激活的蛋白激酶级联反应。遗传证据表明，Ste5必须低聚才能发挥功能，但其对Ste5功能和定位的影响尚不清楚。在这里，我们表明低聚影响Ste5活性和本地化。 Ste5的大部分是单体的，这表明低聚反应受到严格调节。增加Ste5寡聚体的库会增加与Ste11的结合。值得注意的是，Ste5低聚物还可以更有效地从细胞核输出，被Ste11保留在细胞质中，并更好地募集到质膜，从而导致交配的促分裂原活化蛋白激酶级联反应的组成性活化。共沉淀测试表明，RING-H2结构域是寡聚化的关键决定因素。突变分析表明，富含亮氨酸的结构域限制了RING-H2结构域的可及性，并且除了促进Ste11缔合和激活外，还抑制了出口和募集。我们的结果表明，Ste5的主要形式是具有不可访问的RING-H2结构域和Ste11结合位点的非活性单体，而活性形式是一种更有效地输出和募集且具有更易于访问的RING-H2域和Ste11的寡聚体。结合位点。 [参考：46]

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