Definition of the human mitochondrial TOM interactome reveals TRABD as a new interacting protein

The mitochondrial proteome arises from dual genetic origins. Nuclear-encoded proteins need to be transported across or inserted into two distinguished membranes, and the translocase of the outer mitochondrial membrane (TOM) complex represents the main translocase in the outer mitochondrial membrane. Its composition and regulation have been extensively investigated within yeast cells. However, we have little knowledge of the TOM complex composition within human cells. Here, we have defined the TOM interactome in a comprehensive manner using biochemical approaches to isolate the TOM complex in combination with quantitative mass spectrometry analyses. With these studies, we defined the pleiotropic nature of the human TOM complex, including new interactors, such as TRABD. Our studies provide a framework to understand the various biogenesis pathways that merge at the TOM complex within human cells.

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Publication Details

Journal
Journal of Cell Science
Published
2025-03-19
DOI
https://doi.org/10.1242/jcs.263576
Citations
3
Primary Topic
Mitochondrial Function and Pathology
Type
article
Field-Weighted Citation Impact
2.42

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Definition of the human mitochondrial TOM interactome reveals TRABD as a new interacting protein

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Definition of the human mitochondrial TOM interactome reveals TRABD as a new interacting protein

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article en
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Abstract

The mitochondrial proteome arises from dual genetic origins. Nuclear-encoded proteins need to be transported across or inserted into two distinguished membranes, and the translocase of the outer mitochondrial membrane (TOM) complex represents the main translocase in the outer mitochondrial membrane. Its composition and regulation have been extensively investigated within yeast cells. However, we have little knowledge of the TOM complex composition within human cells. Here, we have defined the TOM interactome in a comprehensive manner using biochemical approaches to isolate the TOM complex in combination with quantitative mass spectrometry analyses. With these studies, we defined the pleiotropic nature of the human TOM complex, including new interactors, such as TRABD. Our studies provide a framework to understand the various biogenesis pathways that merge at the TOM complex within human cells.

Journal of Cell ScienceVol. 138(9)
University of Freiburg (DE), University of Würzburg (DE), University of Göttingen (DE)
Deutsche Forschungsgemeinschaft, Volkswagen Foundation
Life in Land
Openalex Percentile: Top 12%
Mitochondrial Function and Pathology
2.42
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