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首页> 美国卫生研究院文献>The Plant Cell >Targeting of a Nicotiana plumbaginifolia H+-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants
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Targeting of a Nicotiana plumbaginifolia H+-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants

机译：缺省情况下将Nicotiana plumbaginifolia H + -ATPase靶向血浆膜不是必需的并且需要胞质结构决定簇

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摘要

The structural determinants involved in the targeting of multitransmembrane-span proteins to the plasma membrane (PM) remain poorly understood. The plasma membrane H+-ATPase (PMA) from Nicotiana plumbaginifolia, a well-characterized 10 transmembrane–span enzyme, was used as a model to identify structural elements essential for targeting to the PM. When PMA2 and PMA4, representatives of the two main PMA subfamilies, were fused to green fluorescent protein (GFP), the chimeras were shown to be still functional and to be correctly and rapidly targeted to the PM in transgenic tobacco. By contrast, chimeric proteins containing various combinations of PMA transmembrane spanning domains accumulated in the Golgi apparatus and not in the PM and displayed slow traffic properties through the secretory pathway. Individual deletion of three of the four cytosolic domains did not prevent PM targeting, but deletion of the large loop or of its nucleotide binding domain resulted in GFP fluorescence accumulating exclusively in the endoplasmic reticulum. The results show that, at least for this polytopic protein, the PM is not the default pathway and that, in contrast with single-pass membrane proteins, cytosolic structural determinants are required for correct targeting.
机译：涉及跨膜蛋白靶向质膜​​（PM）的结构决定因素仍然知之甚少。烟草（Nicotiana plumbaginifolia）的质膜H + -ATPase（PMA）是一种特征鲜明的10跨膜跨度酶，被用作模型来鉴定靶向PM所必需的结构元件。当两个主要PMA亚家族的代表PMA2和PMA4与绿色荧光蛋白（GFP）融合时，显示嵌合体仍然有效，并且可以正确，快速地靶向转基因烟草中的PM。相反，包含PMA跨膜结构域各种组合的嵌合蛋白在高尔基体而不是PM中积累，并通过分泌途径表现出缓慢的运输特性。四个胞质结构域中的三个的单独缺失不能阻止PM靶向，但是大环或其核苷酸结合结构域的缺失导致GFP荧光仅在内质网中积累。结果表明，至少对于该多聚体蛋白而言，PM不是默认途径，并且与单次通过膜蛋白相反，胞浆结构决定簇是正确靶向所必需的。

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