The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
The mitochondrial UPR – protecting organelle protein homeostasis
Abstract
Mitochondria are required for numerous essential metabolic processes including the regulation of apoptosis; therefore, proper maintenance of the mitochondrial proteome is crucial. The protein-folding environment in mitochondria is challenged by organelle architecture, the presence of reactive oxygen species and the difficulties associated with assembly of the electron transport chain, which consists of components encoded by both the mitochondrial and the nuclear genomes. Mitochondria have dedicated molecular chaperones and proteases that promote proper protein folding, complex assembly and quality control. Work in cultured mammalian cells and Caenorhabditis elegans has yielded clues to the mechanisms linking perturbations in the protein-folding environment in the mitochondrial matrix to the expression of nuclear genes encoding mitochondrial proteins. Here, we review the current knowledge of this mitochondrial unfolded protein response (UPRmt), compare it with the better understood UPR of the endoplasmic reticulum and highlight its potential impact on development and disease.
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Cites
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Cited by
Mitochondria: In Sickness and in Health
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Molecular chaperones in protein folding and proteostasis
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Ageing as a risk factor for neurodegenerative disease
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Mitonuclear protein imbalance as a conserved longevity mechanism
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Metadata
- Authors
- Haynes, C. M., & Ron, D.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2010-11-15
- Volume
- 123
- Issue
- 22
- Pages
- 3849-3855
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2019881443
- Cited by
- 494
- References
- 57
- FWCI
- 11.90
- Type
- journal article
- Language
- en
- Open access
- closed
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