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YME 1L degradation reduces mitochondrial proteolytic capacity during oxidative stress
Author(s) -
Rainbolt T Kelly,
Saunders Jaclyn M,
Wiseman R Luke
Publication year - 2015
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201438976
Subject(s) - library science , chemistry , physiology , medicine , computer science
Mitochondrial proteostasis is maintained by a network of ATP ‐dependent quality control proteases including the inner membrane protease YME 1L. Here, we show that YME 1L is a stress‐sensitive mitochondrial protease that is rapidly degraded in response to acute oxidative stress. This degradation requires reductions in cellular ATP and involves the activity of the ATP ‐independent protease OMA 1. Oxidative stress‐dependent reductions in YME 1L inhibit protective YME 1L‐dependent functions and increase cellular sensitivity to oxidative insult. Collectively, our results identify stress‐induced YME 1L degradation as a biologic process that attenuates protective regulation of mitochondrial proteostasis and promotes cellular death in response to oxidative stress.