The Ubiquitin-Proteasome System Regulates Mitochondrial Intermembrane Space Proteins
Open accessAbstract
Mitochondrial precursor proteins are synthesized in the cytosol and subsequently imported into mitochondria. The import of mitochondrial intermembrane space proteins is coupled with their oxidative folding and governed by the mitochondrial intermembrane space import and assembly (MIA) pathway. The cytosolic steps that precede mitochondrial import are not well understood. We identified a role for the ubiquitin-proteasome system in the biogenesis of intermembrane space proteins. Interestingly, the function of the ubiquitin-proteasome system is not restricted to conditions of mitochondrial protein import failure. The ubiquitin-proteasome system persistently removes a fraction of intermembrane space proteins under physiological conditions, acting as a negative regulator in the biogenesis of this class of proteins. Thus, the ubiquitin-proteasome system plays an important role in determining the levels of proteins targeted to the intermembrane space of mitochondria.
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Unfolded IMS proteins can exit the IMS through the TOM translocase.
“Moreover, unfolded IMS proteins can exit the IMS through the TOM translocase, which is the same route used for import [40].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [40]
In mouse cardiac muscle, the UPS ubiquitinates several OMM, IMS, and matrix mitochondrial proteins.
“In mouse cardiac muscle, the UPS ubiquitinates several OMM, IMS, and matrix mitochondrial proteins [39, 40].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [40]
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- Authors
- Bragoszewski, P., Gornicka, A., Sztolsztener, M. E., & Chacinska, A.
- Affiliations
- International Institute of Molecular and Cell Biology, Warsaw, Poland
- International Institute of Molecular and Cell Biology (PL)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2013-06-01
- Volume
- 33
- Issue
- 11
- Pages
- 2136-2148
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3648063
- OpenAlex
- W2168290116
- Cited by
- 149
- References
- 70
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 2 · 2023: 21 · 2022: 7 · 2021: 10 · 2020: 22 · 2019: 16 · 2018: 8 · 2017: 10 · 2016: 10 · 2015: 17 · 2014: 5 · 2013: 5
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Narodowym Centrum Nauki
- European Regional Development Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- ubiquitin-proteasome system, mitochondrial intermembrane space, mitochondrial protein import, oxidative protein folding, protein biogenesis, protein degradation
- MeSH terms
- Copper Transport Proteins, Mitochondrial Precursor Protein Import Complex Proteins, Cytosol, Intracellular Membranes, Leupeptins, Membrane Proteins, Mitochondria, Multienzyme Complexes, Mutation, Molecular Chaperones, Ubiquitin, Membrane Transport Proteins, Cation Transport Proteins, Saccharomyces cerevisiae Proteins, Mitochondrial Membrane Transport Proteins, Proteasome Endopeptidase Complex, Ubiquitinated Proteins
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