Cytosolic domain of the human mitochondrial fission protein Fis1 adopts a TPR fold
Cytosolic domain of the human mitochondrial fission protein Fis1 adopts a TPR fold
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DOI：
10.1002/prot.10524
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发表时间：
2004-01-01
影响因子：
2.9
通讯作者：
Gittis, AG
中科院分区：
文献类型：
--
作者：
Dohm, JA;Lee, SJ;Gittis, AG
线粒体是多态性结构，在细胞分化、衰老和凋亡中具有重要作用。线粒体通过融合和分裂在细胞中建立不同的形状和分布来适应这种不同的功能。1因此，介导裂变的组分可能是细胞内和细胞外信号的靶点，这些信号在各种基本细胞过程中调节线粒体活性。2Fis1、Mdv1和Dnm1是最近发现的3个酿酒酵母线粒体分裂所必需的蛋白质。Mdv1和Dnm1以Fis1依赖的方式组装在线粒体外膜上。2 Dnm1是一种动力蛋白相关的GT3，推测其寡聚化以在收缩部位的线粒体小管外表面周围形成环，类似于其同系物动力蛋白在胞吞作用期间形成的结构。3 Mdv1与Fis1和Dnm1结合，被认为在裂变过程的后期起作用。4
Mitochondria are polymorphic structures with fundamental roles in cellular differentiation, aging, and apoptosis. Mitochondria accommodate such diverse functions by establishing varying shapes and distributions in the cell via fusion and fission. 1 Thus, the components that mediate fission are likely to be targets for intracellular and extracellular signals that modulate mitochondrial activity in a variety of essential cellular processes. 2Fis1, Mdv1, and Dnm1 are three recently identified proteins essential for the fission of mitochondria in Saccharomyces cerevisiae. Mdv1 and Dnm1 assemble in a Fis1-dependent manner on the mitochondrial outer membrane. 2 Dnm1 is a dynamin-related GTPase that presumably oligomerizes to form rings around the outer surface of the mitochondrial tubules at sites of constriction, similar to structures formed during endocytosis by its homologue dynamin. 3 Mdv1 associates with Fis1 and Dnm1 and is thought to act late in the fission process. 4