Requirement for Nudel and dynein for assembly of the lamin B spindle matrix.
Requirement for Nudel and dynein for assembly of the lamin B spindle matrix.
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DOI：
10.1038/ncb1832
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发表时间：
2009-03
影响因子：
21.3
通讯作者：
Zheng, Yixian
中科院分区：
文献类型：
--
作者：
Ma, Li;Tsai, Ming-Ying;Wang, Shusheng;Lu, Bingwen;Chen, Rong;Yates, John R., III;Zhu, Xueliang;Zheng, Yixian
鸟苷三磷酸酶Ran （RanGTP）可以刺激V型中间丝蛋白（lamin B）组装成膜状的lamin B纺锤体基质，这是纺锤体组装过程中微管组织所必需的。微管反过来又增强了基质的组装。我们在这里报告，孤立的矩阵包含已知的主轴装配因子，如动力蛋白和努德尔。利用爪蟾卵提取物的纺锤体组装试验，我们发现Nudel在纺锤体组装过程中调节微管组织，而不依赖于其在着丝点上的功能。重要的是，Nudel直接与层粘连蛋白B相互作用，以动力蛋白依赖的方式促进含有层粘连蛋白B的基质在微管上的积累和组装。干扰Nudel或dynein均可抑制层粘连蛋白B基质的组装。然而，耗尽层粘连蛋白B仍然允许形成含有动力蛋白和Nudel的基质。因此，dynein和Nudel调节层粘连蛋白B矩阵的组装。有趣的是，我们发现消耗层粘连蛋白B导致纺锤体和纺锤极紊乱，而破坏Nudel或dynein的功能导致纺锤极完全没有聚焦。我们认为，Nudel调节微管组织，部分是通过促进层粘胶蛋白B纺锤体基质以动力蛋白依赖的方式组装。
Guanosine triphosphatase Ran (RanGTP) can stimulate assembly of the type V intermediate filament protein, lamin B, into a membranous lamin B spindle matrix, which is required for proper microtubule organization during spindle assembly. Microtubules in turn enhance assembly of the matrix. We report here that the isolated matrix contains known spindle assembly factors such as dynein and Nudel. Using spindle assembly assays in Xenopus egg extracts, we show that Nudel regulates microtubule organization during spindle assembly independent of its function at kinetochores. Importantly, Nudel directly interacts with lamin B to facilitate the accumulation and assembly of lamin B-containing matrix on microtubules in a dynein-dependent manner. Perturbing either Nudel or dynein inhibited assembly of lamin B matrix. However, depleting lamin B still allowed formation of matrices containing dynein and Nudel. Therefore, dynein and Nudel regulate assembly of the lamin B matrix. Interestingly, we found that whereas depleting lamin B resulted in disorganized spindle and spindle poles, disrupting the function of Nudel or dynein caused a complete lack of spindle pole focusing. We suggest that Nudel regulates microtubule organization in part by facilitating assembly of the lamin B spindle matrix in a dynein-dependent manner.
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