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Sam50 Functions in Mitochondrial Intermembrane Space Bridging and Biogenesis of Respiratory Complexes
Abstract
Mitochondria possess an outer membrane (OMM) and an inner membrane (IMM), which folds into invaginations called cristae. Lipid composition, membrane potential, and proteins in the IMM influence organization of cristae. Here we show an essential role of the OMM protein Sam50 in the maintenance of the structure of cristae. Sam50 is a part of the sorting and assembly machinery (SAM) necessary for the assembly of β-barrel proteins in the OMM. We provide evidence that the SAM components exist in a large protein complex together with the IMM proteins mitofilin and CHCHD3, which we term the mitochondrial intermembrane space bridging (MIB) complex. Interactions between OMM and IMM components of the MIB complex are crucial for the preservation of cristae. After destabilization of the MIB complex, we observed deficiency in the assembly of respiratory chain complexes. Long-term depletion of Sam50 influences the amounts of proteins from all large respiratory complexes that contain mitochondrially encoded subunits, pointing to a connection between the structural integrity of cristae, assembly of respiratory complexes, and/or the maintenance of mitochondrial DNA (mtDNA).
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In the citing paper
“This aberrant shape of cristae was previously found to be associated with mitochondrial dysfunction [41,42,45,46]”
From Mitochondrial Dysfunction in Human Leukemic Stem/Progenitor Cells upon Loss of RAC2 (2015) · cites this paper as [41]
In the citing paper
“Recent studies showed that depletion of SAM50 and another mitochondrial membrane protein, mitofilin, resulted in disorganized cristae, morphologically similar to the phenotype we observed upon RAC2 downregulation [41,45,46].”
From Mitochondrial Dysfunction in Human Leukemic Stem/Progenitor Cells upon Loss of RAC2 (2015) · cites this paper as [41]
In the citing paper
“Two of those proteins, SAM50 and Metaxin 1 function within the SAM complex, involved in incorporation of proteins to the mitochondrial outer membrane, as well as regulating cristae stability (Fig 5A) [41,42].”
From Mitochondrial Dysfunction in Human Leukemic Stem/Progenitor Cells upon Loss of RAC2 (2015) · cites this paper as [41]
In the citing paper
“Interestingly, depletion of these proteins resulted not only in a deficient assembly of the MRC complexes, but it also altered the expression of several genes involved in oxidative phosphorylation [41].”
From Mitochondrial Dysfunction in Human Leukemic Stem/Progenitor Cells upon Loss of RAC2 (2015) · cites this paper as [41]
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Cited by
Mitochondrial proteins: from biogenesis to functional networks
Pfanner, N., Warscheid, B., & Wiedemann, N. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0092-0 · Cited by 1,028
Mitochondrial Cristae: Where Beauty Meets Functionality
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Mitochondrial Dysfunction in Human Leukemic Stem/Progenitor Cells upon Loss of RAC2
Capala, M. E., Maat, H., Bonardi, F., van den Boom, V., Kuipers, J., Vellenga, E., Giepmans, B. N. G., & Schuringa, J. J. (2015) · PLOS ONE · doi:10.1371/journal.pone.0128585 · Cited by 20
Metadata
- Authors
- Ott, C., Ross, K., Straub, S., Thiede, B., Götz, M., Goosmann, C., Krischke, M., Mueller, M. J., Krohne, G., Rudel, T., & Kozjak-Pavlovic, V.
- Affiliations
- Biocenter, Chair of Microbiology, University of Würzburg, Würzburg, Germany
- Department of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany
- The Biotechnology Centre of Oslo, University of Oslo, Oslo, Norway
- Microscopy Core Facility, Max Planck Institute for Infection Biology, Berlin, Germany
- Biocenter, Chair of Pharmaceutical Biology, University of Würzburg, Würzburg, Germany
- Biocenter, Central Department for Electron Microscopy, University of Würzburg, Würzburg, Germany
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2012-03-01
- Volume
- 32
- Issue
- 6
- Pages
- 1173-1188
- ISSN
- 1098-5549
- Cited by
- 228
- References
- 5
- Language
- en
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