Cited by 247Advanced Proteomics Techniques and ApplicationsMitochondrial Function and PathologyMass Spectrometry Techniques and Applications

Proteomic analysis of the mouse liver mitochondrial inner membrane

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Da Cruz, Sandrine, Xenarios, Ioannis, Langridge, James, Vilbois, Francis, Parone, Phillipe A., Martinou, Jean-Claude·2003·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1074/jbc.m304940200

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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
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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