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Mitochondrial protein import: from proteomics to functional mechanisms

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 11, Issue 9, Pages 655-667

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm2959

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Funding

  1. Deutsche Forschungsgemeinschaft
  2. Excellence Initiative of the German Federal and State Governments [EXC 294 BIOSS, GSC-4]
  3. Trinationales Graduiertenkolleg [GRK 1478]
  4. Bundesministerium fur Bildung und Forschung
  5. Sonderforschungsbereich [746]
  6. Landesforschungspreis Baden-Wurttemberg
  7. Fonds der Chemischen Industrie

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Mitochondria contain similar to 1,000 different proteins, most of which are imported from the cytosol. Two import pathways that direct proteins into the mitochondrial inner membrane and matrix have been known for many years. The identification of numerous new transport components in recent proteomic studies has led to novel mechanistic insight into these pathways and the discovery of new import pathways into the outer membrane and intermembrane space. Protein translocases do not function as independent units but are integrated into dynamic networks and are connected to machineries that function in bioenergetics, mitochondrial morphology and coupling to the endoplasmic reticulum.

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