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The ArfGAP2/3 Glo3 and ergosterol collaborate in transport of a subset of cargoes

机译:ArfGAP2 / 3 Glo3和麦角甾醇合作运输部分货物

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摘要

Proteins reach the plasma membrane through the secretory pathway in which the trans Golgi network (TGN) acts as a sorting station. Transport from the TGN to the plasma membrane is maintained by a number of different pathways that act either directly or via the endosomal system. Here we show that a subset of cargoes depends on the ArfGAP2/3 Glo3 and ergosterol to maintain their proper localization at the plasma membrane. While interfering with neither ArfGAP2/3 activity nor ergosterol biosynthesis individually significantly altered plasma membrane localization of the tryptophan transporter Tat2, the general amino acid permease Gap1 and the v-SNARE Snc1, in a Δ glo3 Δ erg3 strain those proteins accumulated in internal endosomal structures. Export from the TGN to the plasma membrane and recycling from early endosomes appeared unaffected as the chitin synthase Chs3 that travels along these routes was localized normally. Our data indicate that a subset of proteins can reach the plasma membrane efficiently but after endocytosis becomes trapped in endosomal structures. Our study supports a role for ArfGAP2/3 in recycling from endosomes and in transport to the vacuole/lysosome.
机译:蛋白质通过分泌途径到达质膜,反式高尔基体网络(TGN)在其中充当分拣站。从TGN到质膜的转运通过许多直接或通过内体系统起作用的不同途径来维持。在这里,我们显示了一部分货物依赖于ArfGAP2 / 3 Glo3和麦角固醇来维持其在质膜上的适当定位。在既不干扰ArfGAP2 / 3活性又不干扰麦角固醇的生物合成的情况下,它们分别显着改变了色氨酸转运蛋白Tat2,普通氨基酸渗透酶Gap1和v-SNARE Snc1的质膜定位,这些蛋白在Δglo3Δerg3菌株中积累在内体结构中。由于沿这些途径传播的几丁质合酶Chs3已正常定位,因此从TGN出口到质膜和从早期内体中回收似乎没有受到影响。我们的数据表明,蛋白质的一个子集可以有效地到达质膜,但是在胞吞作用被困在内体结构中之后。我们的研究支持ArfGAP2 / 3在从内体循环和转运到液泡/溶酶体中的作用。

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