The protective role of yeast Cathepsin D in acetic acid-induced apoptosis depends on ANT (Aac2p) but not on the voltage-dependent channel (Por1p)
The protective role of yeast Cathepsin D in acetic acid-induced apoptosis depends on ANT (Aac2p) but not on the voltage-dependent channel (Por1p)
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DOI：
10.1016/j.febslet.2012.11.025
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发表时间：
2013-01-16
期刊：
影响因子：
3.5
通讯作者：
Corte-Real, Manuela
中科院分区：
文献类型：
--
作者：
Pereira, Helena;Azevedo, Flavio;Corte-Real, Manuela
我们以前已经证明，在醋酸诱导的细胞凋亡过程中，酵母组织蛋白D(CatD)Pep4p从空泡转移到胞浆，是有效降解线粒体所必需的，尽管它在这一过程中的具体作用仍不清楚。在这里，我们证明了Pep4p在醋酸诱导的细胞凋亡中的保护作用依赖于它的催化活性，并且不依赖于酵母电压依赖的阴离子通道Por1p(它对线粒体的降解没有作用)，但依赖于酵母腺嘌呤核苷酸转运体AAC蛋白。我们的结果表明，酵母空泡CatD和参与细胞凋亡调控的线粒体蛋白之间存在着不同的相互作用。(C)2012年欧洲生化学会联合会。爱思唯尔出版公司版权所有。
We have previously shown that the yeast Cathepsin D (CatD) Pep4p translocates from the vacuole to the cytosol during acetic acid-induced apoptosis and is required for efficient mitochondrial degradation, though its specific role in this process is still elusive. Here, we show that the protective role of Pep4p in acetic acid-induced apoptosis depends on its catalytic activity and is independent of the yeast voltage-dependent anion channel Por1p (which has no role on mitochondrial degradation) but dependent on AAC proteins, the yeast adenine nucleotide translocator. Our results demonstrate a differential interplay between yeast vacuolar CatD and mitochondrial proteins involved in apoptosis regulation. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.