Otera Hidenori, Mihara Katsuyoshi
Department of Molecular Biology; Graduate School of Medical Science; Kyushu University; Kyushu, Fukuoka Japan.
Small GTPases. 2011 May;2(3):167-172. doi: 10.4161/sgtp.2.3.16486.
Mitochondria frequently change their morphology by fusion and fission, and these dynamic morphologic changes are essential for maintaining both mitochondrial and cellular functions. The cytoplasmic dynamin-related guanosine triphosphatase (GTPase) Drp1 (Dnm1 in yeast) is recruited to mitochondrial fission sites and severs mitochondria. Although the mitochondrial outer membrane (MOM) protein Fis1 functions as a membrane receptor for Dnm1 in yeast, it is not yet known whether the human homolog of yeast Fis1 (hFis1) is a membrane receptor for Drp1 in mammals. We recently identified the C-tail anchored MOM protein Mff as the bona fide receptor essential for recruiting Drp1 to mitochondrial fission sites. Here, we focus on this key molecule for mitochondrial fission after a brief description of the proteins involved in mitochondrial fission and fusion reactions. Finally, we discuss the expected role of hFis1 for regulating the mitochondrial dynamics in mammals.
线粒体经常通过融合和分裂来改变其形态,而这些动态的形态变化对于维持线粒体和细胞功能至关重要。细胞质中与发动蛋白相关的鸟苷三磷酸酶(GTP酶)Drp1(酵母中的Dnm1)被招募到线粒体分裂位点并使线粒体分裂。虽然线粒体外膜(MOM)蛋白Fis1在酵母中作为Dnm1的膜受体发挥作用,但目前尚不清楚酵母Fis1的人类同源物(hFis1)在哺乳动物中是否是Drp1的膜受体。我们最近鉴定出C末端锚定的MOM蛋白Mff是将Drp1招募到线粒体分裂位点所必需的真正受体。在此,在简要描述参与线粒体分裂和融合反应的蛋白质后,我们将重点关注这个线粒体分裂的关键分子。最后,我们讨论hFis1在调节哺乳动物线粒体动态方面的预期作用。