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首页> 外文期刊>Nature cell biology >Gamma-tubulin complex-mediated anchoring of spindle microtubules to spindle-pole bodies requires Msd1 in fission yeast.
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Gamma-tubulin complex-mediated anchoring of spindle microtubules to spindle-pole bodies requires Msd1 in fission yeast.

机译:γ-微管蛋白复合物介导的纺锤体微管对纺锤极体的锚定需要裂殖酵母中的Msd1。

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摘要

The anchoring of microtubules to subcellular structures is critical for cell polarity and motility. Although the process of anchoring cytoplasmic microtubules to the centrosome has been studied in some detail, it is not known how spindle microtubules are anchored to the mitotic centrosome and, particularly, whether anchoring and nucleation of mitotic spindles are functionally separate. Here, we show that a fission yeast coiled-coil protein, Msd1, is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body (SPB). msd1 deletion causes spindle microtubules to abnormally extend beyond SPBs, which results in chromosome missegregation. Importantly, this protruding spindle is phenocopied by the amino-terminal deletion mutant of Alp4, a component of the gamma-tubulin complex (gamma-TuC), which lacks the potential Msd1-interacting domain. We propose that Msd1 interacts with gamma-TuC, thereby specifically anchoring the minus end of microtubules to SPBs without affecting microtubule nucleation.
机译:微管对亚细胞结构的锚定对于细胞极性和运动性至关重要。尽管已经详细研究了将细胞质微管锚定到中心体的过程,但是还不知道纺锤体微管如何锚定到有丝分裂中心体,尤其是有丝分裂纺锤体的锚定和成核在功能上是分开的。在这里,我们显示裂变酵母卷曲螺旋蛋白Msd1是将纺锤体微管的负端锚定到中心体等同物纺锤体(SPB)所必需的。 msd1缺失导致纺锤体微管异常延伸超过SPB,从而导致染色体错聚。重要的是,这个突出的纺锤由Alp4的氨基末端缺失突变体表型复制,Alp4是缺乏潜在的Msd1相互作用域的γ-微管蛋白复合物(gamma-TuC)的组成部分。我们建议Msd1与γ-TuC进行交互,从而将微管的负端特异性锚定到SPB,而不会影响微管成核。

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