A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos.
A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos.
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DOI：
10.1083/jcb.140.4.897
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发表时间：
1998-02-23
期刊：
影响因子：
--
通讯作者：
Miller KG
中科院分区：
文献类型：
--
作者：
Lantz VA;Miller KG
摘要。细胞组织的协调需要细胞骨架细丝系统的相互作用。最近，一些研究表明，细胞成分沿微管和肌动蛋白丝的运输对细胞组织和功能很重要。我们在这里报告了可能介导肌动蛋白和微管细胞骨架之间协调的分子。我们已经鉴定出一种195-kD蛋白，它与一类肌球蛋白（果蝇95F非常规肌球蛋白）共免疫沉淀。编码195-kD蛋白的基因的克隆和测序表明，它是细胞质连接蛋白(CLIP) -170的第一个同源物，CLIP -170是一种连接内噬泡和微管的蛋白质。我们将该蛋白命名为D-CLIP-190（预测分子质量为189 kD），基于其与CLIP-170的相似性以及与微管共同沉积的能力。D-CLIP-190和CLIP-170之间的相似性延伸到蛋白质的整个长度，并且它们具有许多共同的预测序列和结构特征。95F肌球蛋白和D-CLIP-190在果蝇胚胎发生过程中在许多组织中共表达。在神经元的轴突中，它们位于相同的颗粒结构中，类似于囊泡。它们也在早期胚胎的后极共定位，这种定位依赖于肌动蛋白细胞骨架。肌凝蛋白和微管结合蛋白的同源物在神经系统和后极的关联，其中微管和肌动蛋白依赖过程已知是重要的，使我们推测这两种蛋白可能在功能上连接肌动蛋白和微管细胞骨架。
Abstract. Coordination of cellular organization requires the interaction of the cytoskeletal filament systems. Recently, several lines of investigation have suggested that transport of cellular components along both microtubules and actin filaments is important for cellular organization and function. We report here on molecules that may mediate coordination between the actin and microtubule cytoskeletons. We have identified a 195-kD protein that coimmunoprecipitates with a class VI myosin, Drosophila 95F unconventional myosin. Cloning and sequencing of the gene encoding the 195-kD protein reveals that it is the first homologue identified of cytoplasmic linker protein (CLIP)–170, a protein that links endocytic vesicles to microtubules. We have named this protein D-CLIP-190 (the predicted molecular mass is 189 kD) based on its similarity to CLIP-170 and its ability to cosediment with microtubules. The similarity between D-CLIP-190 and CLIP-170 extends throughout the length of the proteins, and they have a number of predicted sequence and structural features in common. 95F myosin and D-CLIP-190 are coexpressed in a number of tissues during embryogenesis in Drosophila. In the axonal processes of neurons, they are colocalized in the same particulate structures, which resemble vesicles. They are also colocalized at the posterior pole of the early embryo, and this localization is dependent on the actin cytoskeleton. The association of a myosin and a homologue of a microtubule-binding protein in the nervous system and at the posterior pole, where both microtubule and actin-dependent processes are known to be important, leads us to speculate that these two proteins may functionally link the actin and microtubule cytoskeletons.
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