线粒体分裂
生物
膜间隙
线粒体
细胞生物学
外膜转位酶
线粒体膜间隙
线粒体载体
内膜转移酶
线粒体融合
DNM1L型
DNAJA3公司
裂变
线粒体凋亡诱导通道
ATP-ADP转位酶
线粒体膜转运蛋白
线粒体内膜
线粒体DNA
生物化学
细菌外膜
物理
大肠杆菌
量子力学
基因
中子
作者
Olivia M. Connor,Srujan K. Matta,Jonathan R. Friedman
标识
DOI:10.1083/jcb.202303147
摘要
Mitochondria are highly dynamic double membrane–bound organelles that maintain their shape in part through fission and fusion. Mitochondrial fission is performed by a dynamin-related protein, Dnm1 (Drp1 in humans), that constricts and divides the mitochondria in a GTP hydrolysis–dependent manner. However, it is unclear whether factors inside mitochondria help coordinate the process and if Dnm1/Drp1 activity is sufficient to complete the fission of both mitochondrial membranes. Here, we identify an intermembrane space protein required for mitochondrial fission in yeast, which we propose to name Mdi1 (also named Atg44). Loss of Mdi1 causes mitochondrial hyperfusion due to defects in fission, but not the lack of Dnm1 recruitment to mitochondria. Mdi1 is conserved in fungal species, and its homologs contain an amphipathic α-helix, mutations of which disrupt mitochondrial morphology. One model is that Mdi1 distorts mitochondrial membranes to enable Dnm1 to robustly complete fission. Our work reveals that Dnm1 cannot efficiently divide mitochondria without the coordinated function of Mdi1 inside mitochondria.
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