In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-04-20)
Abstract:
Our cells contain compartments called mitochondria, which provide energy and serve as a home for many metabolic pathways that are critical for life. Changes in mitochondrial activity can contribute to aging and to the development of several age-associated diseases. However, our cells contain systems that detect changes in the performance of mitochondria and can act to re-establish a healthy state. These systems respond to stress or changes in metabolism by degrading particular proteins in the mitochondria. This enables damaged or unwanted proteins to be replaced with new proteins, but it is not clear how these mitochondrial defense systems work to keep mitochondria healthy as an organism ages. Budding yeast is a good model in which to study the aging process because the performance of this yeast’s mitochondria change in a characteristic way as the yeast ages. Previous studies have shown that these changes are caused by alterations in another cell structure called the lysosome, which can store nutrients and is where many proteins are degraded. Here, Hughes et al. used yeast cells to investigate how mitochondrial defense systems operate during aging. The experiments reveal an entirely new mitochondrial protein degradation system that helps to keep the mitochondria healthy as the yeast cells age. This process is rapidly triggered by changes in lysosome activity and results in certain proteins in each mitochondrion being sorted into a small compartment made from a part of the mitochondrion. This compartment is released from the mitochondrion and then travels to the lysosome where the proteins are destroyed. Inhibiting the formation of these compartments results in mitochondria being more sensitive to cellular stress. The next steps following on from this work are to find out exactly what role this mitochondrial defense pathway plays in cells and why it targets only a small set of all the proteins found in mitochondria.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.13943.001
DOI:
10.7554/eLife.13943.002
DOI:
10.7554/eLife.13943.003
DOI:
10.7554/eLife.13943.004
DOI:
10.7554/eLife.13943.005
DOI:
10.7554/eLife.13943.006
DOI:
10.7554/eLife.13943.007
DOI:
10.7554/eLife.13943.008
DOI:
10.7554/eLife.13943.009
DOI:
10.7554/eLife.13943.010
DOI:
10.7554/eLife.13943.011
DOI:
10.7554/eLife.13943.012
DOI:
10.7554/eLife.13943.013
DOI:
10.7554/eLife.13943.014
DOI:
10.7554/eLife.13943.015
DOI:
10.7554/eLife.13943.016
DOI:
10.7554/eLife.13943.017
DOI:
10.7554/eLife.13943.018
DOI:
10.7554/eLife.13943.019
DOI:
10.7554/eLife.13943.020
DOI:
10.7554/eLife.13943.021
DOI:
10.7554/eLife.13943.022
DOI:
10.7554/eLife.13943.023
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2016
detail.hit.zdb_id:
2687154-3