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Proteomics

Reducing mitochondrial mysteries

Nature Chemical Biology volume 20, pages 132–133 (2024)Cite this article

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Defining subcellular locations and interacting partners for proteins accelerates their functional characterization. A new in vivo tagging approach achieves both for mitochondrial matrix proteins and helps connect a key oxidoreductase to coenzyme Q biosynthesis.

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Fig. 1: Mitochondrial matrix-specific proximity labeling identifies RTN4IP1 as a novel oxidoreductase involved in CoQ biosynthesis.

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Authors and Affiliations

  1. Department of Cell Biology & Physiology, Washington University School of Medicine, St. Louis, MO, USA

    Rachel M. Guerra & David J. Pagliarini

  2. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA

    Rachel M. Guerra & David J. Pagliarini

  3. Department of Genetics, Washington University School of Medicine, St. Louis, MO, USA

    Rachel M. Guerra & David J. Pagliarini

Authors
  1. Rachel M. Guerra
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  2. David J. Pagliarini
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Correspondence to David J. Pagliarini.

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The authors declare no competing interests.

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Guerra, R.M., Pagliarini, D.J. Reducing mitochondrial mysteries. Nat Chem Biol 20, 132–133 (2024). https://doi.org/10.1038/s41589-023-01435-x

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