The mitochondrial unfolded protein response — synchronizing genomes

Maintenance of the mitochondrial proteome is performed primarily by chaperones, which fold and assemble proteins, and by proteases, which degrade excess damaged proteins. Upon various types of mitochondrial stress, triggered genetically or pharmacologically, dysfunction of the proteome is sensed and...

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Bibliographic Details
Published in:Current opinion in cell biology 2015-04, Vol.33, p.74-81
Main Authors: Jovaisaite, Virginija, Auwerx, Johan
Format: Article
Language:English
Subjects:
Aging
Animals
Cell Nucleus - genetics
Cell Nucleus - metabolism
Cytoprotection
Genome - genetics
Genome, Mitochondrial - genetics
Humans
Internal Medicine
Mammals
Mitochondria - genetics
Mitochondria - metabolism
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Proteome - genetics
Proteome - metabolism
Signal Transduction - genetics
Unfolded Protein Response - genetics
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Summary:Maintenance of the mitochondrial proteome is performed primarily by chaperones, which fold and assemble proteins, and by proteases, which degrade excess damaged proteins. Upon various types of mitochondrial stress, triggered genetically or pharmacologically, dysfunction of the proteome is sensed and communicated to the nucleus, where an extensive transcriptional program, aimed to repair the damage, is activated. This feedback loop, termed the mitochondrial unfolded protein response (UPRmt ), synchronizes the activity of the mitochondrial and nuclear genomes and as such ensures the quality of the mitochondrial proteome. Here we review the recent advances in the UPRmt field and discuss its induction, signaling, communication with the other mitochondrial and major cellular regulatory pathways, as well as its potential implications on health and lifespan.
ISSN:0955-0674
1879-0410
DOI:10.1016/j.ceb.2014.12.003