Dnm1 forms spirals that are structurally tailored to fit mitochondria.
Dnm1 forms spirals that are structurally tailored to fit mitochondria.
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DOI：
10.1083/jcb.200506078
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发表时间：
2005-09-26
影响因子：
7.8
通讯作者：
Nunnari, Jodi
中科院分区：
文献类型：
--
作者：
Ingerman, Elena;Perkins, Edward M;Marino, Michael;Mears, Jason A;McCaffery, J Michael;Hinshaw, Jenny E;Nunnari, Jodi
动力蛋白相关蛋白（Dynamin-related proteins，DRPs）是一类自组装的GTP酶，其共同功能是调节细胞膜动力学。Dnm 1是一种酵母DRP（人类的Drp 1/Dlp 1），是线粒体分裂所必需的，但其机制尚不清楚。我们提供的证据表明，Dnm 1可能通过自组装来驱动与线粒体分裂相关的膜收缩事件。还确定了Dnm 1自组装的两个调节特征。Dnm 1自组装通过限速成核步骤进行，组装的Dnm 1结构的核苷酸水解相对于GTP是高度合作的。Dnm 1形成扩展的螺旋，其直径大于发动蛋白-1的螺旋，但其大小，显着地，在体内的线粒体收缩部位是相等的。这些数据表明，Dnm 1已经进化形成了适合线粒体尺寸的结构。
Dynamin-related proteins (DRPs) are large self-assembling GTPases whose common function is to regulate membrane dynamics in a variety of cellular processes. Dnm1, which is a yeast DRP (Drp1/Dlp1 in humans), is required for mitochondrial division, but its mechanism is unknown. We provide evidence that Dnm1 likely functions through self-assembly to drive the membrane constriction event that is associated with mitochondrial division. Two regulatory features of Dnm1 self-assembly were also identified. Dnm1 self-assembly proceeded through a rate-limiting nucleation step, and nucleotide hydrolysis by assembled Dnm1 structures was highly cooperative with respect to GTP. Dnm1 formed extended spirals, which possessed diameters greater than those of dynamin-1 spirals but whose sizes, remarkably, were equal to those of mitochondrial constriction sites in vivo. These data suggest that Dnm1 has evolved to form structures that fit the dimensions of mitochondria.