生物
细胞生物学
线粒体分裂
线粒体
AAA蛋白
线粒体融合
跨膜结构域
内膜转移酶
突变体
线粒体内膜
内膜
线粒体基质
跨膜蛋白
线粒体载体
胞浆
ATP酶
线粒体膜转运蛋白
细菌外膜
线粒体DNA
氨基酸
生物化学
受体
基因
酶
大肠杆菌
作者
Benoît Gilquin,Emmanuel Taillebourg,Nadia Cherradi,Arnaud Hubstenberger,Olivia Gay,Nicolas S. Merle,Nicole Assard,Marie-Odile Fauvarque,Shiho Tomohiro,Osamu Kuge,Jacques Baudier
摘要
Dynamic interactions between components of the outer (OM) and inner (IM) membranes control a number of critical mitochondrial functions such as channeling of metabolites and coordinated fission and fusion. We identify here the mitochondrial AAA(+) ATPase protein ATAD3A specific to multicellular eukaryotes as a participant in these interactions. The N-terminal domain interacts with the OM. A central transmembrane segment (TMS) anchors the protein in the IM and positions the C-terminal AAA(+) ATPase domain in the matrix. Invalidation studies in Drosophila and in a human steroidogenic cell line showed that ATAD3A is required for normal cell growth and cholesterol channeling at contact sites. Using dominant-negative mutants, including a defective ATP-binding mutant and a truncated 50-amino-acid N-terminus mutant, we showed that ATAD3A regulates dynamic interactions between the mitochondrial OM and IM sensed by the cell fission machinery. The capacity of ATAD3A to impact essential mitochondrial functions and organization suggests that it possesses unique properties in regulating mitochondrial dynamics and cellular functions in multicellular organisms.
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