Mitochondrial proteins articles within Nature

Featured

  • Article
    | Open Access

    Tim17 contains conserved negative charges close to the intermembrane space side of the bilayer, which are essential to initiate presequence protein translocation along a distinct transmembrane cavity of Tim17 for both classes of preproteins.

    • Laura F. Fielden
    • , Jakob D. Busch
    •  & Nils Wiedemann

  • Review Article |

    The functional and regulatory aspects of the ‘mitochondrial divisome’ are separated into core and accessory machinery, thus providing a mechanistic understanding of the process of mitochondrial fission.

    • Felix Kraus
    • , Krishnendu Roy
    •  & Michael T. Ryan

  • Article |

    In Saccharomyces cerevisiae, Ubx2 promotes clearing trapped precursor proteins from the channel of the translocase of the outer membrane, in a translocation-associated degradation pathway that maintains the protein import capacity of mitochondria.

    • Christoph U. Mårtensson
    • , Chantal Priesnitz
    •  & Thomas Becker

  • Letter |

    Electron cryomicroscopy structures are provided for all core and supernumerary protein subunits of mammalian complex I, a 45-subunit enzyme that powers eukaryotic respiration.

    • Jiapeng Zhu
    • , Kutti R. Vinothkumar
    •  & Judy Hirst

  • Letter |

    Mitochondrial dysfunction and cellular protein homeostasis failure are hallmarks of many diseases and age-associated pathologies; this study shows that the mitochondrial import defect of nuclear-encoded proteins triggers a cellular pathway, termed unfolded protein response activated by mistargeting of proteins (UPRam), that acts to minimize the stress caused by non-imported mitochondrial precursor proteins in order to sustain cellular protein homeostasis and organismal fitness.

    • Lidia Wrobel
    • , Ulrike Topf
    •  & Agnieszka Chacinska

  • Letter |

    Mitochondria are shown to form a conductive pathway throughout the cell in the form of a proton motive force, and throughout this network, mitochondrial protein localization seems to be varied, allowing optimized generation and utilization of the mitochondrial membrane potential; the rapid energy distribution network, which depends on conduction rather than diffusion, could explain how the muscle can rapidly respond to energy demands.

    • Brian Glancy
    • , Lisa M. Hartnell
    •  & Robert S. Balaban

  • Article |

    The uptake of calcium by mitochondria has a central role in cell physiology, and an imbalance can trigger cell death. Now the first protein that is localized to the mitochondrion and is specifically required for calcium uptake has been identified. This protein, mitochondrial calcium uptake 1 (MICU1), represents the founding member of a set of proteins required for high-capacity calcium uptake. Its discovery should aid in the full molecular characterization of the mitochondrial calcium uptake pathways.

    • Fabiana Perocchi
    • , Vishal M. Gohil
    •  & Vamsi K. Mootha

  • Letter |

    During fasting SIRT3 is induced in liver and brown adipose tissue. One of SIRT3's substrates is shown to be long–chain acyl co-enzyme A dehydrogenase (LCAD). Without SIRT3 LCAD becomes hyperacetylated, which diminishes its activity, and reduces fatty acid oxidation. Mice without SIRT3 have all the hallmarks of fatty acid oxidation disorders during fasting, including reduced ATP levels and intolerance to cold. Thus, acetylation is a novel regulatory mechanism for fatty acid oxidation.

    • Matthew D. Hirschey
    • , Tadahiro Shimazu
    •  & Eric Verdin

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