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酿酒酵母Arc35p通过两种基因可分离的钙调蛋白功能来调节肌动蛋白和微管细胞骨架。

Saccharomyces cerevisiae Arc35p works through two genetically separable calmodulin functions to regulate the actin and tubulin cytoskeletons.

作者信息

Schaerer-Brodbeck C, Riezman H

机构信息

Biozentrum of the University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

出版信息

J Cell Sci. 2000 Feb;113 ( Pt 3):521-32. doi: 10.1242/jcs.113.3.521.

Abstract

Analysis of the arc35-1 mutant has revealed previously that this component of the Arp2/3 complex is involved in organization of the actin cytoskeleton. Further characterization uncovered a cell division cycle phenotype with arrest as large-budded cells. Cells with correctly positioned metaphase spindles accumulated at the restrictive temperature. The observed metaphase arrest most likely occurs by activation of the spindle assembly checkpoint, because arc35-1 was synthetically lethal with a deletion of BUB2. Arc35p activity is required late in G(1) for its cell cycle function. Both the actin and microtubule defects of arc35-1 can be suppressed by overexpression of calmodulin. Analysis of a collection of ts cmd1 mutants for their ability to suppress the actin and/or microtubule defect revealed that the two defects observed in arc35-1 are genetically separable. These data suggest that the actin defect is probably not the cause of the microtubule defect.

摘要

对arc35-1突变体的分析先前已揭示,Arp2/3复合物的这一组成部分参与肌动蛋白细胞骨架的组织。进一步的表征发现了一种细胞分裂周期表型,即细胞停滞在大芽期。在限制温度下,中期纺锤体定位正确的细胞会积累。观察到的中期停滞很可能是通过纺锤体组装检查点的激活而发生的,因为arc35-1与BUB2缺失具有合成致死性。Arc35p活性在G(1)晚期是其细胞周期功能所必需的。钙调蛋白的过表达可以抑制arc35-1的肌动蛋白和微管缺陷。对一组温度敏感的cmd1突变体抑制肌动蛋白和/或微管缺陷能力的分析表明,在arc35-1中观察到的两种缺陷在遗传上是可分离的。这些数据表明,肌动蛋白缺陷可能不是微管缺陷的原因。

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