Format

Send to

Choose Destination
EMBO Rep. 2015 Jan;16(1):97-106. doi: 10.15252/embr.201438976. Epub 2014 Nov 27.

YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress.

Author information

1
Department of Molecular & Experimental Medicine, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA.
2
Department of Molecular & Experimental Medicine, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA wiseman@scripps.edu.

Abstract

Mitochondrial proteostasis is maintained by a network of ATP-dependent quality control proteases including the inner membrane protease YME1L. Here, we show that YME1L 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 OMA1. Oxidative stress-dependent reductions in YME1L inhibit protective YME1L-dependent functions and increase cellular sensitivity to oxidative insult. Collectively, our results identify stress-induced YME1L degradation as a biologic process that attenuates protective regulation of mitochondrial proteostasis and promotes cellular death in response to oxidative stress.

KEYWORDS:

AAA protease; YME1L; mitochondrial proteostasis; oxidative stress

PMID:
25433032
PMCID:
PMC4304733
DOI:
10.15252/embr.201438976
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center