Regulation of mitochondrial inner membrane fusion: divergent evolution with similar solutions?
Regulation of mitochondrial inner membrane fusion: divergent evolution with similar solutions?
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DOI：
10.1007/s00294-015-0542-6
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发表时间：
2015
期刊：
影响因子：
2.5
通讯作者：
J. Wagener
中科院分区：
文献类型：
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作者：
J. Wagener
线粒体的连续融合和分裂决定了线粒体的动态形状。线粒体融合的一个重要因素是保守的内膜动力蛋白样GTP酶Mgm1/OPA1。这种蛋白的有限蛋白分解被认为是从线粒体网络中分离并随后消除功能障碍部分的一种机制。在这里，我将简要总结我们目前对哺乳动物、面包酵母、裂殖酵母、黑腹果蝇和烟曲霉等潜在的蛋白质分解加工步骤的了解。在所分析的物种中，Mgm1/OPA1处理的明显差异表明在线粒体内膜融合的调控中存在令人惊讶的机制异质性。
Continuous mitochondrial fusion and fission define the dynamic shape of mitochondria. One essential player of mitochondrial fusion is the conserved inner membrane dynamin-like GTPase Mgm1/OPA1. Limited proteolysis of this protein has been proposed as a mechanism to separate and subsequently eliminate dysfunctional parts from the mitochondrial network. Here, I briefly summarize our current knowledge about the underlying proteolytic processing steps in mammals, baker’s yeast,Schizosaccharomyces pombe,Drosophila melanogasterandAspergillus fumigatus. The apparent great diversity in Mgm1/OPA1 processing among the analyzed species indicates a surprising mechanistic heterogeneity in the regulation of mitochondrial inner membrane fusion.