Proteomic analysis of the mouse liver mitochondrial inner membrane
Open accessAbstract
Mitochondria play a crucial role in cellular homeostasis, which justifies the increasing interest in mapping the different components of these organelles. Here we have focused our study on the identification of proteins of the mitochondrial inner membrane (MIM). This membrane is of particular interest because, besides the well known components of the respiratory chain complexes, it contains several ion channels and many carrier proteins that certainly play a key role in mitochondrial function and, therefore, deserve to be identified at the molecular level. To achieve this goal we have used a novel approach combining the use of highly purified mouse liver mitochondrial inner membranes, extraction of membrane proteins with organic acid, and two-dimensional liquid chromatography coupled to tandem mass spectrometry. This procedure allowed us to identify 182 proteins that are involved in several biochemical processes, such as the electron transport machinery, the protein import machinery, protein synthesis, lipid metabolism, and ion or substrate transport. The full range of isoelectric point (3.9-12.5), molecular mass (6-527 kDa), and hydrophobicity values (up to 16 transmembrane predicted domains) were represented. In addition, of the 182 proteins found, 20 were unknown or had never previously been associated with the MIM. Overexpression of some of these proteins in mammalian cells confirmed their mitochondrial localization and resulted in severe remodeling of the mitochondrial network. This study provides the first proteome of the MIM and provides a basis for a more detailed study of the newly characterized proteins of this membrane.
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ATAD3A localizes to mitochondria and appears to be involved in mitochondrial membrane dynamics.
“Several studies have localized ATAD3A to the mitochondria (143, 144), where is appears to be involved in mitochondrial membrane dynamics.”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [144]
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- Authors
- Da Cruz, S., Xenarios, I., Langridge, J., Vilbois, F., Parone, P. A., & Martinou, J.-C.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Martinou, Jean-Claude
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 42
- Pages
- 41566-41571
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2139514626
- Cited by
- 247
- References
- 24
- Citations by year
- 2025: 3 · 2024: 6 · 2023: 3 · 2022: 3 · 2021: 10 · 2020: 5 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 3 · 2015: 12 · 2014: 11 · 2013: 17 · 2012: 15
- FWCI
- 6.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- inner mitochondrial membrane, mouse liver mitochondria, mitochondrial proteome, membrane protein identification, respiratory chain complexes, ion channels, carrier proteins, lipid metabolism, mitochondrial network remodeling, mitochondrial localization
- MeSH terms
- Animals, Cations, Cell Membrane, Cell Survival, Chromatography, Liquid, Cloning, Molecular, Female, HeLa Cells, Humans, Immunohistochemistry, Intracellular Membranes, Liver, Mitochondria, Mass Spectrometry, Protein Structure, Tertiary, Proteome, Spectrometry, Mass, Electrospray Ionization, Mice
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