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Surveying the mitochondrial proteome

Nature Cell Biology volume 23, pages 1216–1217 (2021)Cite this article

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Mitochondrial-derived vesicles (MDVs) transfer mitochondrial content to lysosomes and peroxisomes. A study now reveals that MDVs deliver β-barrel proteins and fully assembled mitochondrial complexes for lysosomal degradation, establishing an important role for MDVs in mitochondrial protein quality control.

Mitochondrial function and biogenesis depends on import, folding and assembly of more than 1,000 different proteins. Different quality control systems monitor mitochondrial proteostasis, which is pivotal for maintenance of the mitochondrial proteome. On the mitochondrial surface, factors of the ubiquitin–proteasome system remove defective or mislocalized proteins as well as precursor proteins that are stalled during import in the translocase of the outer mitochondrial membrane (TOM) complex. Several intramitochondrial proteases degrade damaged proteins in the matrix, the intermembrane space and the inner membrane. While these mechanisms target individual proteins, mitochondrial-derived vesicles (MDVs) and piecemeal mitophagy are removing mitochondrial sections and even entire damaged organelles (in the case of mitophagy)1. In this issue of Nature Cell Biology, König et al.2 report on an analysis of the proteome of purified MDVs to define their content and unravel essential steps underlying MDV formation.

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Fig. 1: Function and formation of MDVs.

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Authors and Affiliations

  1. Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany

    Dominic Winter & Thomas Becker

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  1. Dominic Winter
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  2. Thomas Becker
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Correspondence to Thomas Becker.

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The authors declare no competing interests.

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Winter, D., Becker, T. Surveying the mitochondrial proteome. Nat Cell Biol 23, 1216–1217 (2021). https://doi.org/10.1038/s41556-021-00801-y

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