蛋白质稳态
细胞生物学
线粒体
线粒体内膜
生物
去极化
内膜
内膜转移酶
生物物理学
化学
线粒体膜转运蛋白
作者
T. Kelly Rainbolt,Justine Lebeau,Cristina Puchades,R. Luke Wiseman
出处
期刊:Cell Reports
[Elsevier]
日期:2016-03-01
卷期号:14 (9): 2041-2049
被引量:132
标识
DOI:10.1016/j.celrep.2016.02.011
摘要
The mitochondrial inner membrane proteases YME1L and OMA1 are critical regulators of essential mitochondrial functions, including inner membrane proteostasis maintenance and mitochondrial dynamics. Here, we show that YME1L and OMA1 are reciprocally degraded in response to distinct types of cellular stress. OMA1 is degraded through a YME1L-dependent mechanism in response to toxic insults that depolarize the mitochondrial membrane. Alternatively, insults that depolarize mitochondria and deplete cellular ATP stabilize active OMA1 and promote YME1L degradation. We show that the differential degradation of YME1L and OMA1 alters their proteolytic processing of the dynamin-like GTPase OPA1, a critical regulator of mitochondrial inner membrane morphology, which influences the recovery of tubular mitochondria following membrane-depolarization-induced fragmentation. Our results reveal the differential stress-induced degradation of YME1L and OMA1 as a mechanism for sensitively adapting mitochondrial inner membrane protease activity and function in response to distinct types of cellular insults.
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