A novel direct interaction of endoplasmic reticulum with microtubules
A novel direct interaction of endoplasmic reticulum with microtubules
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DOI：
10.1093/emboj/17.21.6168
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发表时间：
1998-11-02
期刊：
影响因子：
11.4
通讯作者：
Hauri, HP
中科院分区：
文献类型：
--
作者：
Klopfenstein, DRC;Kappeler, F;Hauri, HP
真核细胞中细胞器的定位和动力学关键取决于膜-细胞骨架的相互作用。马达蛋白在细胞器膜沿着微管定向运动中起重要作用，但膜与微管细胞骨架稳定相互作用的基本机制在很大程度上是未知的。在这里，我们报告，p63，一个完整的膜蛋白的网状亚结构域的粗面内质网（ER），结合微管在体内和体外。p63在细胞培养中的过表达导致了ER的显著重排，并伴随着微管沿着改变的ER成束。对p63胞质结构域的突变分析揭示了负责这些变化的两个决定因素：靠近N-末端的ER重排决定因素和中心微管结合区。对应于p63的胞质尾区的肽在体外促进微管聚合。p63是第一个被发现的能将膜细胞器与微管直接连接的膜蛋白，它可能有助于内质网沿着微管的定位。
The positioning and dynamics of organelles in eukaryotic cells critically depend on membrane-cytoskeleton interactions. Motor proteins play an important role in the directed movement of organelle membranes along microtubules, but the basic mechanism by which membranes stably interact with Che microtubule cytoskeleton is largely unknown. Here we report that p63, an integral membrane protein of the reticular subdomain of the rough endoplasmic reticulum (ER), binds microtubules in vivo and in vitro. Overexpression of p63 in cell culture led to a striking rearrangement of the ER and to concomitant bundling of microtubules along the altered ER, Mutational analysis of the cytoplasmic domain of p63 revealed two determinants responsible for these changes: an ER rearrangement determinant near the N-terminus and a central microtubule-binding region, The two determinants function independently of one another as indicated by deletion experiments. A peptide corresponding to the cytoplasmic tail of p63 promoted microtubule polymerization in vitro. p63 is the first identified integral membrane protein that can link a membrane organelle directly to microtubules, By doing so, it may contribute to the positioning of the ER along microtubules.