Dynamin assembly strategies and adaptor proteins in mitochondrial fission.

Dynamin assembly strategies and adaptor proteins in mitochondrial fission.
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DOI:
10.1016/j.cub.2013.08.040
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发表时间:
2013-10-07
期刊:
影响因子:
9.2
通讯作者:
Shaw, Janet M.
Shaw, Janet M.
中科院分区:
生物学1区
文献类型:
--
作者:
Bui, Huyen T.;Shaw, Janet M.

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线粒体的分裂是由一个动力相关的GTdR介导的,GTdR在细胞器的收缩部位组装。这种GTdR在裂变中的机制与经典的发动蛋白有关,后者切断了质膜上网格蛋白包被的小坑的颈部。虽然这些膜重塑事件的规模不同的数量级,结构研究揭示了经典和线粒体动力蛋白,以适应这些差异的装配性能的变化。尽管取得了这一进展,但结构和机制模型尚未纳入越来越多的线粒体动力蛋白的膜募集和功能所需的衔接蛋白。在这里,我们回顾了酵母和哺乳动物线粒体动力蛋白的结构和组装特性,并讨论了已知的衔接蛋白的活动。
Mitochondrial fission is mediated by a dynamin-related GTPase that assembles at constricted sites on the organelle. The mechanism of this GTPase in fission is related to that of classical dynamin, which severs the necks of clathrin-coated pits at the plasma membrane. Although the scale of these membrane remodeling events differs by an order of magnitude, structural studies reveal variations in the assembly properties of classical and mitochondrial dynamins that accommodate these differences. Despite this progress, structural and mechanistic models have not yet incorporated a growing number of adaptor proteins required for the membrane recruitment and function of mitochondrial dynamins. Here we review the structure and assembly properties of the yeast and mammalian mitochondrial dynamins and discuss what is known about the activities of their adaptor proteins.
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