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首页> 外文期刊>EMBO Journal >The small GTP binding protein rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin.
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The small GTP binding protein rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin.

机译:小三磷酸鸟苷结合蛋白rab7是至关重要的幽门螺杆菌引起的细胞空泡形成螺杆菌细胞毒素。

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摘要

The VacA cytotoxin, produced by toxigenic strains of Helicobacter pylori, induces the formation of large vacuoles highly enriched in the small GTPase rab7. To probe the role of rab7 in vacuolization, HeLa cells were transfected with a series of rab mutants and exposed to VacA. Dominant-negative mutants of rab7 effectively prevented vacuolization, whereas homologous rab5 and rab9 mutants were only partially inhibitory or ineffective, respectively. Expression of wild-type or GTPase-deficient rab mutants synergized with VacA in inducing vacuolization. In vitro fusion of late endosomes was enhanced by active rab7 and inhibited by inactive rab7, consistent with vacuole formation by merging of late endosomes in a process that requires functional rab7. Taken together, the effects of overexpressed rab proteins described here indicate that continuous membrane flow along the endocytic pathway is necessary for vacuole growth.
机译:VacA细胞毒素,由产毒素的菌株幽门螺杆菌,诱发的形成大的高纯度的小液泡GTPase rab7。液泡化,海拉细胞转染一系列的rab突变体和暴露于VacA。显性负rab7有效的突变体预防液泡化,而同源rab5和rab9突变体只有部分抑制分别或无效。野生型或GTPase-deficient rab突变体主体性与诱导VacA液泡化。体外的核内体融合是增强了活跃rab7和不活跃的rab7抑制,与液泡的形成通过合并一致过程,需要后期核内体功能性rab7。过表达rab这里描述的蛋白质表明,连续膜流沿液泡内吞作用的途径是必要的增长。

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