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首页> 外文期刊>Molecular biology of the cell >Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton
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Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton

机译：维利丁（Villidin）是一种来自盘基网柄菌的新型WD重复和与维林有关的蛋白，与膜和细胞骨架有关。

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Villidin is a novel multidomain protein (190 kDa) from Dictyostelium amoebae containing WD repeats at its N-terminus, three PH domains in the middle of the molecule, and five gelsolin-like segments at the C-terminus, followed by a villin-like headpiece. Villidin mRNA and protein are present in low amounts during growth and early aggregation, but increase during development and reach their highest levels at the tipped mound stage. The protein is present in the cytosol as well as in the cytoskeletal and membrane fractions. GFP-tagged full-length villidin exhibits a similar distribution as native villidin, including a distinct colocalization with Golgi structures. Interestingly, GFP fusions with the gelsolin/villin-like region are uniformly dispersed in the cytoplasm, whereas GFP fusions of the N-terminal WD repeats codistribute with F-actin and are associated with the Triton-insoluble cytoskeleton. Strains lacking villidin because of targeted deletion of its gene grow normally and can develop into fruiting bodies. However, cell motility is reduced during aggregation and phototaxis is impaired in the mutant strains. We conclude that villidin harbors a major F-actin binding site in the N-terminal domain and not in the villin-like region as expected; association of villidin with vesicular membranes suggests that the protein functions as a linker between membranes and the actin cytoskeleton. [References: 64]
机译：Villidin是一种新的多域蛋白（190 kDa），来自变形杆菌，在其N端包含WD重复序列，在分子中部包含三个PH结构域，在C端包含五个凝溶胶蛋白样片段，随后是villin样蛋白头巾。绒毛蛋白mRNA和蛋白质在生长和早期聚集时少量存在，但在发育过程中会增加并在小丘阶段达到最高水平。该蛋白质存在于细胞质以及细胞骨架和膜级分中。 GFP标记的全长绒毛蛋白表现出与天然绒毛蛋白相似的分布，包括与高尔基体结构的明显共定位。有趣的是，具有凝溶胶蛋白/ villin样区域的GFP融合物均匀地分散在细胞质中，而N末端WD的重复序列的GFP融合物与F-肌动蛋白共分布并且与Triton不溶性细胞骨架有关。由于其基因的定向缺失而缺乏维里丁的菌株正常生长，并且可以发育成子实体。然而，在突变菌株中细胞运动性降低并且趋光性受损。我们得出的结论是，vilildin在N末端域中具有主要的F-肌动蛋白结合位点，而不是预期的在villin样区域中。绒毛蛋白与水泡膜的缔合表明该蛋白起着膜与肌动蛋白细胞骨架之间的连接子的作用。 [参考：64]

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