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首页> 外文期刊>Cell biology international. >Yeast dynamin and Ypt6 function in parallel for the endosome‐to‐Golgi retrieval of Snc1
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Yeast dynamin and Ypt6 function in parallel for the endosome‐to‐Golgi retrieval of Snc1

机译：酵母发电机和YPT6并行用于SNC1的内部组到高尔基检索

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摘要

Abstract Protein recycling is an important cellular process required for cell homeostasis. Results from prior studies have shown that vacuolar sorting protein‐1 (Vps1), a dynamin homolog in yeast, is implicated in protein recycling from the endosome to the trans ‐Golgi Network (TGN). However, the function of Vps1 in relation to Ypt6, a master GTPase in the recycling pathway, remains unknown. The present study reveals that Vps1 physically interacts with Ypt6 if at least one of them is full‐length. We found that overexpression of full‐length Vps1, but not GTP hydrolysis‐defective Vps1 mutants, is sufficient to rescue abnormal phenotypes of Snc1 distribution provoked by the loss of Ypt6, and vice versa. This suggests that Vps1 and Ypt6 function in parallel pathways instead of in a sequential pathway and that GTP binding/hydrolysis of Vps1 is required for proper traffic of Snc1 toward the TGN. Additionally, we identified two novel Vps1‐binding partners, Vti1 and Snc2, which function for the endosome‐derived vesicle fusion at the TGN. Taken together, the present study demonstrates that Vps1 plays a role in later stages of the endosome‐to‐TGN traffic.
机译：摘要蛋白质再循环是细胞稳态所需的重要细胞过程。本研究结果表明，真空分选蛋白-1（VPS1），酵母中的动力学同源物，涉及从内部组的蛋白质再循环到反式 - 原酚网络（TGN）。然而，VPS1与YPT6相关的vps1，母gptpase在回收通路中仍然未知。本研究表明，如果其中至少一个是全长，则VPS1与YPT6物理相互作用。我们发现全长VPS1的过度表达，但不是GTP水解缺陷的VPS1突变体，足以拯救因YPT6损失引起的SNC1分布的异常表型，反之亦然。这表明vps1和ypt6在并联途径中的功能而不是在顺序路径中，并且需要vps1的GPT结合/水解，以便对TGn进行适当的SNC1流量。此外，我们鉴定了两种新的VPS1结合伴侣，VTI1和SNC2，其在TGN处于内体衍生的囊泡融合。在一起，本研究表明，VPS1在内部到TGN交通的后期发挥作用。

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