Although general anesthesia is indispensable during modern surgical procedures, the mechanism by which inhalation anesthetics act on the synaptic membrane at the molecular and cellular level is largely unknown. In this study, we used yeast cells to examine the effect of isoflurane, an inhalation anesthetic, on membrane proteins. Bap2, an amino acid transporter localized on the plasma membrane, was endocytosed when yeast cells were treated with isoflurane. Depletion of RSP5, an E3 ligase, prevented this endocytosis and Bap2 was ubiquitinated in response to isoflurane, indicating an ubiquitin-dependent process. Screening all the Rsp5 binding adaptors showed that Art2 plays a central role in this process. These results suggest that isoflurane affects Bap2 via an Art2-Rsp5-dependent ubiquitination system.

中文翻译：

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异氟醚诱导酵母中 Bap2 的 Art2-Rsp5 依赖性内吞作用

尽管在现代外科手术中全身麻醉是必不可少的，但吸入麻醉剂在分子和细胞水平上作用于突触膜的机制在很大程度上是未知的。在这项研究中，我们使用酵母细胞来检查异氟醚（一种吸入麻醉剂）对膜蛋白的影响。当酵母细胞用异氟醚处理时，Bap2 是一种位于质膜上的氨基酸转运蛋白，它被内吞。RSP5 （一种 E3 连接酶）的消耗阻止了这种内吞作用，并且 Bap2 响应于异氟醚而泛素化，表明存在泛素依赖性过程。筛选所有 Rsp5 结合适配器表明 Art2 在此过程中起着核心作用。这些结果表明异氟醚通过依赖 Art2-Rsp5 的泛素化系统影响 Bap2。