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Salt Stress-Induced Disassembly of Arabidopsis Cortical Microtubule Arrays Involves 26S Proteasome-Dependent Degradation of SPIRAL1

机译:盐胁迫诱导的拟南芥皮层微管阵列的拆卸涉及26S蛋白酶体依赖的SPIRAL1降解。

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The dynamic instability of cortical microtubules (MTs) (i.e., their ability to rapidly alternate between phases of growth and shrinkage) plays an essential role in plant growth and development. In addition, recent studies have revealed a pivotal role for dynamic instability in the response to salt stress conditions. The salt stress response includes a rapid depolymerization of MTs followed by the formation of a new MT network that is believed to be better suited for surviving high salinity. Although this initial depolymerization response is essential for the adaptation to salt stress, the underlying molecular mechanism has remained largely unknown. Here, we show that the MT-associated protein SPIRAL1 (SPR1) plays a key role in salt stress-induced MT disassembly. SPR1, a microtubule stabilizing protein, is degraded by the 26S proteasome, and its degradation rate is accelerated in response to high salinity. We show that accelerated SPR1 degradation is required for a fast MT disassembly response to salt stress and for salt stress tolerance.
机译:皮质微管(MTs)的动态不稳定性(即它们在生长期和萎缩阶段之间快速交替的能力)在植物生长和发育中起着至关重要的作用。此外,最近的研究表明,在盐胁迫条件下动态不稳定性起着关键作用。盐胁迫响应包括MT的快速解聚,然后形成新的MT网络,该网络被认为更适合于保持高盐度。尽管这种初始的解聚反应对于适应盐胁迫至关重要,但其潜在的分子机制仍然很大程度上未知。在这里,我们显示MT相关蛋白SPIRAL1(SPR1)在盐胁迫诱导的MT拆卸中起关键作用。 SPS1是一种微管稳定蛋白,可被26S蛋白酶体降解,并且响应高盐度可加快其降解速度。我们表明,加速的SPR1降解是快速MT拆卸对盐胁迫和盐胁迫耐受性所必需的。

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