植物er成形GTPase RHD3的独特和保守特征。

Cellular logistics Pub Date : 2014-01-01 Epub Date: 2014-02-28 DOI:10.4161/cl.28217
Giovanni Stefano, Federica Brandizzi
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引用次数: 16

摘要

内质网(ER)网络的结构完整性取决于膜相关动力蛋白样GTPases的功能,包括后生动物的atlastins、植物的RHD3和酵母的Sey1p。这些蛋白足以驱动重组蛋白脂质体的膜融合,以及功能缺失突变导致明显的内质网形状缺陷的证据表明,atlastins、RHD3和Sey1p促进内质网膜融合。然而,在互失功能背景下的互补实验也表明,RHD3和Sey1p可能在功能上并不等同,这支持了内质网融合机制在真核生物中可能并不完全保守。在这封信中,我们提供了该领域的简要概述以及可能解释植物和酵母er形成动力蛋白样GTPases的功能差异的证据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Unique and conserved features of the plant ER-shaping GTPase RHD3.

The architectural integrity of the endoplasmic reticulum (ER) network depends on the function of membrane-associated dynamin-like GTPases that include metazoan atlastins, plant RHD3 and yeast Sey1p. The evidence that these proteins are sufficient to drive membrane fusion of reconstituted proteoliposomes, and that loss-of-function mutations lead to conspicuous ER shape defects indicates that atlastins, RHD3 and Sey1p promote ER membrane fusion. However, complementation experiments in reciprocal loss-of-function backgrounds have also suggested that RHD3 and Sey1p may be not functionally equivalent, supporting that ER fusion mechanisms may be not entirely conserved in eukaryotes. In this Letter, we provide a brief overview of the field as well as evidence that may explain the functional differences of the plant and yeast ER-shaping dynamin-like GTPases.

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