Release from myosin V via regulated recruitment of an E3 ubiquitin ligase controls organelle localization.
Release from myosin V via regulated recruitment of an E3 ubiquitin ligase controls organelle localization.
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DOI：
10.1016/j.devcel.2014.02.001
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发表时间：
2014-03-10
影响因子：
11.8
通讯作者：
Weisman LS
中科院分区：
文献类型：
--
作者：
Yau RG;Peng Y;Valiathan RR;Birkeland SR;Wilson TE;Weisman LS
分子马达将细胞器运送到特定的亚细胞位置。在到达正确的位置后，马达通过未知的机制释放细胞器。酵母肌球蛋白-V，Myo 2，结合液泡特异性接头Vac 17，将液泡从母细胞运输到芽中。在这里，我们表明，空泡脱离Myo 2发生在多个受管制的步骤沿着整个空泡运输途径。分离起始于母细胞中的Vac 17磷酸化，其募集E3连接酶Dma 1至液泡。然而，Dma 1的募集也需要液泡运输复合体的组装，并且在液泡进入芽后首先观察到。DMA 1一直留在液泡上，直到芽和母液泡分离。随后，Dma 1靶向Vac 17进行蛋白酶体降解。值得注意的是，我们发现，过氧化物酶体运输的终止也需要DMA 1。我们预测，这是一个一般的机制，分离肌球蛋白-V选择货物。
Molecular motors transport organelles to specific subcellular locations. Upon arrival at their correct locations, motors release organelles via unknown mechanisms. The yeast myosin-V, Myo2, binds the vacuole specific adaptor, Vac17, to transport the vacuole from the mother cell to the bud. Here, we show that vacuole detachment from Myo2 occurs in multiple regulated steps along the entire pathway of vacuole transport. Detachment initiates in the mother cell with the phosphorylation of Vac17 which recruits the E3 ligase, Dma1, to the vacuole. However, Dma1 recruitment also requires the assembly of the vacuole transport complex and is first observed after the vacuole enters the bud. Dma1 remains on the vacuole until the bud and mother vacuoles separate. Subsequently, Dma1 targets Vac17 for proteasomal degradation. Notably, we find that the termination of peroxisome transport also requires Dma1. We predict that this is a general mechanism which detaches myosin-V from select cargoes.