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Trends Cell Biol. 2013 Jul;23(7):311-8. doi: 10.1016/j.tcb.2013.02.002. Epub 2013 Mar 13.

Evaluating and responding to mitochondrial dysfunction: the mitochondrial unfolded-protein response and beyond.

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1
Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA. haynesc@mskcc.org

Abstract

During development and cellular differentiation, tissue- and cell-specific programs mediate mitochondrial biogenesis to meet physiological needs. However, environmental and disease-associated factors can perturb mitochondrial activities, requiring cells to adapt to protect mitochondria and maintain cellular homeostasis. Several mitochondrion-to-nucleus signaling pathways, or retrograde responses, have been described, but the mechanisms by which mitochondrial stress or dysfunction is sensed to coordinate precisely the appropriate response has only recently begun to be understood. Recent studies of the mitochondrial unfolded-protein response (UPRmt) indicate that the cell monitors mitochondrial protein import efficiency as an indicator of mitochondrial function. Here, we review how the cell evaluates mitochondrial function and regulates transcriptional induction of the UPRmt, adapts protein-synthesis rates and activates mitochondrial autophagy to promote mitochondrial function and cell survival during stress.

PMID:
23489877
PMCID:
PMC3700555
DOI:
10.1016/j.tcb.2013.02.002
[Indexed for MEDLINE]
Free PMC Article
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