IMiQ: a novel protein quality control compartment protecting mitochondrial functional integrity

Aggregation processes can cause severe perturbations of cellular homeostasis and are frequently associated with diseases. We performed a comprehensive analysis of mitochondrial quality and function in the presence of aggregation-prone polypeptides. Despite a significant aggregate formation inside mi...

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Bibliographic Details
Published in:Molecular biology of the cell 2018-02, Vol.29 (3), p.256-269
Main Authors: Bruderek, Michael, Jaworek, Witold, Wilkening, Anne, Rüb, Cornelia, Cenini, Giovanna, Förtsch, Arion, Sylvester, Marc, Voos, Wolfgang
Format: Article
Language:English
Subjects:
Homeostasis
Mitochondria - metabolism
Mitochondria - pathology
Mitochondria - physiology
Mitochondrial Proteins - physiology
Organelles - metabolism
Peptides
Protein Aggregates - physiology
Protein Folding
Proteostasis Deficiencies - metabolism
Proteostasis Deficiencies - physiopathology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Tetrahydrofolate Dehydrogenase - genetics
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Summary:Aggregation processes can cause severe perturbations of cellular homeostasis and are frequently associated with diseases. We performed a comprehensive analysis of mitochondrial quality and function in the presence of aggregation-prone polypeptides. Despite a significant aggregate formation inside mitochondria, we observed only a minor impairment of mitochondrial function. Detoxification of aggregated reporter polypeptides as well as misfolded endogenous proteins inside mitochondria takes place via their sequestration into a specific organellar deposit site we termed ntra tochondrial protein uality control compartment (IMiQ). Only minor amounts of endogenous proteins coaggregated with IMiQ deposits and neither resolubilization nor degradation by the mitochondrial protein quality control system were observed. The single IMiQ aggregate deposit was not transferred to daughter cells during cell division. Detoxification of aggregates via IMiQ formation was highly dependent on a functional mitochondrial fission machinery. We conclude that the formation of an aggregate deposit is an important mechanism to maintain full functionality of mitochondria under proteotoxic stress conditions.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.e17-01-0027