Contribution of dynein light intermediate and intermediate chains to subcellular localization of the dynein-dynactin motor complex in Schizosaccharomyces pombe
Contribution of dynein light intermediate and intermediate chains to subcellular localization of the dynein-dynactin motor complex in Schizosaccharomyces pombe
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DOI：
10.1111/j.1365-2443.2010.01386.x
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发表时间：
2010-04-01
期刊：
影响因子：
2.1
通讯作者：
Yamamoto, Masayuki
中科院分区：
文献类型：
--
作者：
Fujita, Ikumi;Yamashita, Akira;Yamamoto, Masayuki
在裂殖酵母中，胞质动力蛋白驱动减数分裂前期的振荡核运动，这可能有助于同源染色体的配对。在这里，我们报告了在分裂酵母中鉴定的动力蛋白轻中间链(LIC)，称为Dli1p，并表明Dli1p和动力蛋白中间链(IC)Dic1p对于动力蛋白在减数分裂前期的适当的亚细胞定位和正确的功能是必不可少的。Dli1和dic1基因的表达只在减数分裂细胞中观察到。Dli1p与动力蛋白重链Dhc1p相互作用，共定位。Dli1p的亚细胞定位依赖于Dhc1p，反之亦然。Dhc1p-Dli1p亚复合体可以在不借助Dic1p和dynactin亚单位Ssm4p的情况下定位于纺锤体，但其定位于微管依赖于这两种蛋白。Dic1p依赖于Ssm4p定位于微管，但不定位于Dhc1p和Dli1p。然而，它在SPB上的定位依赖于Dhc1p和Dli1p。Ssm4p在SPB的定位在很大程度上依赖于Dhc1p、Dli1p和Dic1p。因此，Dli1p和Dic1p在将动力蛋白-动力蛋白马达复合体定位到细胞器方面做出了不同的贡献，为了解分裂酵母中动力蛋白亚基的体内功能提供了新的视角。
In fission yeast Schizosaccharomyces pombe, cytoplasmic dynein drives oscillatory nuclear movement during meiotic prophase, which may facilitate pairing of homologous chromosomes. Here, we report the identification of a dynein light intermediate chain (LIC) in fission yeast, termed Dli1p, and show that Dli1p and dynein intermediate chain (IC) Dic1p are essential for the appropriate subcellular localization and proper function of dynein during meiotic prophase. Expression of both the dli1 and dic1 genes was observed only in cells undergoing meiosis. Dli1p interacted and colocalized with dynein heavy chain Dhc1p. The subcellular localization of Dli1p was dependent on Dhc1p, and vice versa. The Dhc1p-Dli1p subcomplex could localize to the spindle pole body (SPB) with no aid of Dic1p and dynactin subunit Ssm4p, but its localization to microtubules was dependent on these two proteins. Dic1p localized to microtubules depending on Ssm4p, but not on Dhc1p and Dli1p. Its localization to the SPB, however, was dependent on Dhc1p and Dli1p. Localization of Ssm4p to the SPB was largely dependent on Dhc1p, Dli1p and Dic1p. Thus, Dli1p and Dic1p contribute differently in localizing the dynein-dynactin motor complex to organelles, providing novel insight into the in vivo function of dynein subunits in fission yeast.