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首页> 外文期刊>Journal of Molecular Biology >Mitochondrial Genome Maintenance 1 (Mgm1) Protein Alters Membrane Topology and Promotes Local Membrane Bending
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Mitochondrial Genome Maintenance 1 (Mgm1) Protein Alters Membrane Topology and Promotes Local Membrane Bending

机译：线粒体基因组维持1（Mgm1）蛋白改变膜的拓扑结构并促进局部膜弯曲

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Large GTPases of the dynamin superfamily promote membrane fusion and division, processes that are crucial for intracellular trafficking and organellar dynamics. To promote membrane scission, dynamin proteins polymerize, wrap around, and constrict the membrane; however, the mechanism underlying their role in membrane fusion remains unclear. We previously reported that the mitochondrial dynamin-related protein mitochondrial genome maintenance 1 (Mgm1) mediates fusion by first tethering opposing membranes and then undergoing a nucleotide-dependent structural transition. However, it is still unclear how Mgm1 directly affects the membrane to drive fusion of tethered membranes. Here, we show that Mgm1 association with the membrane alters the topography of the membrane, promoting local membrane bending. We also demonstrate that Mgm1 creates membrane ruffles resulting in the formation of tubular structures on both supported lipid bilayers and liposomes. These data suggest that Mgm1 membrane interactions impose a mechanical force on the membrane to overcome the hydrophilic repulsion of the phospholipid head groups and initiate the fusion reaction. The work reported here provides new insights into a possible mechanism of Mgm1-driven mitochondrial membrane fusion and sheds light into how members of the dynamin superfamily function as fusion molecules. (C) 2015 Elsevier Ltd. All rights reserved.
机译：发电机超家族的大GTP酶促进膜融合和分裂，这对于细胞内运输和细胞器动力学至关重要。为了促进膜的分裂，动力蛋白聚合，包裹和收缩膜。然而，它们在膜融合中的作用机理尚不清楚。我们以前报道过，线粒体动力蛋白相关蛋白线粒体基因组维护1（Mgm1）通过首先束缚相对的膜，然后经历核苷酸依赖性结构转变来介导融合。但是，仍不清楚Mgm1如何直接影响膜以驱动束缚膜的融合。在这里，我们显示Mgm1与膜的关联会改变膜的形貌，从而促进局部膜的弯曲。我们还证明了Mgm1会产生膜皱纹，从而导致在支持的脂质双层和脂质体上形成管状结构。这些数据表明，Mgm1膜相互作用会在膜上施加机械力，以克服磷脂头基团的亲水排斥并引发融合反应。此处报道的工作为Mgm1驱动的线粒体膜融合的可能机制提供了新见解，并为dynamin超家族成员作为融合分子的功能提供了线索。 （C）2015 Elsevier Ltd.保留所有权利。

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