Loss of glutathione redox homeostasis impairs proteostasis by inhibiting autophagy-dependent protein degradation

@inproceedings{GuerreroGmez2018LossOG,
  title={Loss of glutathione redox homeostasis impairs proteostasis by inhibiting autophagy-dependent protein degradation},
  author={David Alan Guerrero-G{\'o}mez and Jos{\'e} Antonio Mora-Lorca and Beatriz S{\'a}enz-Narciso and Francisco Jos{\'e} Naranjo-Galindo and Fernando Mu{\~n}oz-Lobato and Cristina Parrado-Fern{\'a}ndez and Angel Cedazo-M{\'i}nguez and Christopher D Link and Christian N{\'e}ri and Mar{\'i}a Dolores Sequedo and Rafael P. V{\'a}zquez-Manrique and Elena Fern{\'a}ndez-Su{\'a}rez and Veit Goder and Roser Panet and Elisa Cabiscol and Peter Asjkaer and Juan M. Cabello and Antonio Miranda-Vizuete},
  year={2018}
}
In the presence of aggregation-prone proteins, the cytosol and endoplasmic reticulum (ER) undergo a dramatic shift in their respective redox status, with the cytosol becoming more oxidized and the ER more reducing. However, whether and how changes in the cellular redox status may affect protein aggregation is unknown. Here, we show that C. elegans mutants lacking glutathione reductase gsr-1 gene enhance the deleterious phenotypes of heterologous human as well as endogenous worm aggregation… CONTINUE READING

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