Suppression of tubulin detyrosination by parthenolide recruits the plant-specific kinesin KCH to cortical microtubules.
Suppression of tubulin detyrosination by parthenolide recruits the plant-specific kinesin KCH to cortical microtubules.
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DOI：
10.1093/jxb/erv012
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发表时间：
2015-04
影响因子：
6.9
通讯作者：
Nick P
中科院分区：
文献类型：
--
作者：
Schneider N;Ludwig H;Nick P
通过小白菊内酯处理干扰微管蛋白脱酪氨酸作用，植物特异性驱动蛋白 KCH 对微管的亲和力增加，并导致微管依赖性事件（例如分裂几何形状）的改变。 α-微管蛋白的去酪氨酸化似乎在所有真核生物中都是保守的。然而，其在植物中的生物学功能仍然不清楚。保守的 C 末端酪氨酸被尚未鉴定的微管蛋白酪氨酸羧肽酶 (TTC) 去除，并可以通过微管蛋白酪氨酸连接酶 (TTL) 重新连接。为了深入了解这种脱酪氨酸-酪氨酸循环仍然难以捉摸的生物学功能，我们分析了 TTC 抑制剂小白菊内酯在 BY-2 烟草细胞中的作用。小白菊内酯导致去酪氨酸 α-微管蛋白的消耗，而酪氨酸微管蛋白的水平升高。这种生化效应伴随着循环 BY-2 细胞的生长抑制和微管依赖性事件的改变，这些事件定义了分裂和扩张几何形状，例如细胞板排列或轴向扩张。此外，小白菊内酯引发质外体碱化，表明防御相关的钙流入通道的激活。同时，小白菊内酯促进植物特异性驱动蛋白 KCH 与皮质微管的结合。这些观察结果被整合到一个工作模型中，其中去酪氨酸作为信号来调节参与微管细胞骨架的结构和感觉功能的驱动蛋白马达的结合。
By interfering with tubulin detyrosination via parthenolide treatment, the affinity of the plant-specific kinesin KCH towards microtubules is increased and results in alteration of microtubule-dependent events such as division geometry. Detyrosination of α-tubulin seems to be conserved in all eukaryotes. However, its biological function in plants has remained obscure. A conserved C-terminal tyrosine is removed by a still unidentified tubulin–tyrosine carboxypeptidase (TTC) and can be religated by a tubulin–tyrosine ligase (TTL). To obtain insight into the still elusive biological function of this detyrosination–tyrosination cycle, the effects of the TTC inhibitor parthenolide were analysed in BY-2 tobacco cells. Parthenolide caused a depletion of detyrosinated α-tubulin, whereas the level of tyrosinated tubulin was elevated. This biochemical effect was accompanied by growth inhibition in cycling BY-2 cells and alteration of microtubule-dependent events that define division and expansion geometry such as cell plate alignment or axial expansion. Furthermore, parthenolide triggered an apoplastic alkalinization indicative of activation of defence-related calcium influx channels. At the same time, parthenolide promoted the association of the plant-specific kinesin KCH with cortical microtubules. These observations are integrated into a working model, where detyrosination acts as signal to modulate the binding of kinesin motors involved in structural and sensory functions of the microtubular cytoskeleton.
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