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首页> 外文期刊>Biology Open >Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis
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Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis

机译：内生过程中啤酒酵母信息素受体之间的相互作用

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摘要

This study investigates endocytosis of Saccharomyces cerevisiae α-factor receptor and the role that receptor oligomerization plays in this process. α-factor receptor contains signal sequences in the cytoplasmic C-terminal domain that are essential for ligand-mediated endocytosis. In an endocytosis complementation assay, we found that oligomeric complexes of the receptor undergo ligand-mediated endocytosis when the α-factor binding site and the endocytosis signal sequences are located in different receptors. Both in vitro and in vivo assays suggested that ligand-induced conformational changes in one Ste2 subunit do not affect neighboring subunits. Therefore, recognition of the endocytosis signal sequence and recognition of the ligand-induced conformational change are likely to be two independent events.
机译：这项研究调查了酿酒酵母α因子受体的内吞作用以及受体寡聚在此过程中的作用。 α-因子受体在胞质C末端结构域中包含信号序列，这对于配体介导的内吞作用至关重要。在内吞作用互补测定中，我们发现当α-因子结合位点和内吞信号序列位于不同受体时，受体的寡聚复合物会经历配体介导的内吞作用。体外和体内试验均表明，一个Ste2亚基中配体诱导的构象变化不会影响邻近的亚基。因此，识别胞吞信号序列和识别配体诱导的构象变化可能是两个独立的事件。

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