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Cited by 359Mitochondrial Function and PathologyEndoplasmic Reticulum Stress and DiseaseHeat shock proteins research

Signaling the mitochondrial unfolded protein response

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Pellegrino, Mark W., Nargund, Amrita M., Haynes, Cole M.·2013·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
DOI 10.1016/j.bbamcr.2012.02.019PMC PMC3393825
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Abstract

Mitochondria are compartmentalized organelles essential for numerous cellular functions including ATP generation, iron-sulfur cluster biogenesis, nucleotide and amino acid metabolism as well as apoptosis. To promote biogenesis and proper function, mitochondria have a dedicated repertoire of molecular chaperones to facilitate protein folding and quality control proteases to degrade those proteins that fail to fold correctly. Mitochondrial protein folding is challenged by the complex organelle architecture, the deleterious effects of electron transport chain-generated reactive oxygen species and the mitochondrial genome's susceptibility to acquiring mutations. In response to the accumulation of unfolded or misfolded proteins beyond the organelle's chaperone capacity, cells mount a mitochondrial unfolded protein response (UPR(mt)). The UPR(mt) is a mitochondria-to-nuclear signal transduction pathway resulting in the induction of mitochondrial protective genes including mitochondrial molecular chaperones and proteases to re-establish protein homeostasis within the mitochondrial protein-folding environment. Here, we review the current understanding of UPR(mt) signal transduction and the impact of the UPR(mt) on diseased cells. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids.

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  • Mitochondria communicate with the rest of the cell by metabolite shuttling, direct interactions with other organelles, and altered proteostasis.

    “Mitochondria communicate with the rest of the cell by metabolite shuttling, direct interactions with other organelles, and altered proteostasis [36, 37].”

    From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [37]

    Section 5 describes a pathway in which mitochondrial protein-folding stress is transmitted to the nucleus, supporting communication through altered proteostasis. The passages do not describe metabolite shuttling or direct interactions with other organelles as communication routes. (LLM, conf=0.86)

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Authors
Pellegrino, M. W., Nargund, A. M., & Haynes, C. M.
Affiliations
Memorial Sloan Kettering Cancer Center (US)
Corresponding author
Haynes, Cole M.
ORCID
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2013-02
Volume
1833
Issue
2
Pages
410-416
ISSN
0167-4889 (ISSN-L)
DOI
10.1016/j.bbamcr.2012.02.019
PMC
PMC3393825
OpenAlex
W1984672460
Cited by
359
References
8
Citations by year
2026: 9 · 2025: 13 · 2024: 22 · 2023: 14 · 2022: 21 · 2021: 25 · 2020: 35 · 2019: 31 · 2018: 22 · 2017: 25 · 2016: 46 · 2015: 39 · 2014: 38 · 2013: 16 · 2012: 3
FWCI
2.83
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute on Aging (R01AG040061)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
mitochondrial unfolded protein response, mitochondrial protein folding, mitochondrial chaperone, mitochondrial protease, mitochondrial protein quality control, reactive oxygen species, mitochondrial DNA mutations, mitochondrial biogenesis, mitochondrial protein homeostasis, mitochondrial disease
MeSH terms
Animals, Mitochondria, Signal Transduction, Caenorhabditis elegans, Protein Folding, Molecular Chaperones, Mitochondrial Proteins, Caenorhabditis elegans Proteins, Unfolded Protein Response

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