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  1. Article

    Open Access

    COX17 acetylation via MOF–KANSL complex promotes mitochondrial integrity and function

    Reversible acetylation of mitochondrial proteins is a regulatory mechanism central to adaptive metabolic responses. Yet, how such functionally relevant protein acetylation is achieved remains unexplored. Here ...

    Sukanya Guhathakurta, Niyazi Umut Erdogdu, Juliane J. Hoffmann in Nature Metabolism (2023)

  2. Article

    Author Correction: A multipoint guidance mechanism for β-barrel folding on the SAM complex

    Hironori Takeda, Jon V. Busto, Caroline Lindau in Nature Structural & Molecular Biology (2023)

  3. No Access

    Article

    A multipoint guidance mechanism for β-barrel folding on the SAM complex

    Mitochondrial β-barrel proteins are essential for the transport of metabolites, ions and proteins. The sorting and assembly machinery (SAM) mediates their folding and membrane insertion. We report the cryo-ele...

    Hironori Takeda, Jon V. Busto, Caroline Lindau in Nature Structural & Molecular Biology (2023)

  4. Article

    Open Access

    Mitochondrial complexome reveals quality-control pathways of protein import

    Mitochondria have crucial roles in cellular energetics, metabolism, signalling and quality control14. They contain around 1,000 different proteins that often assemble into complexes and supercomplexes such as re...

    Uwe Schulte, Fabian den Brave, Alexander Haupt, Arushi Gupta, Jiyao Song in Nature (2023)

  5. Article

    Author Correction: Mitochondrial proteins: from biogenesis to functional networks

    A Correction to this paper has been published: https://doi.org/10.1038/s41580-021-00361-x.

    Nikolaus Pfanner, Bettina Warscheid in Nature Reviews Molecular Cell Biology (2021)

  6. No Access

    Article

    Mitochondrial sorting and assembly machinery operates by β-barrel switching

    The mitochondrial outer membrane contains so-called β-barrel proteins, which allow communication between the cytosol and the mitochondrial interior13. Insertion of β-barrel proteins into the outer membrane is me...

    Hironori Takeda, Akihisa Tsutsumi, Tomohiro Nishizawa, Caroline Lindau in Nature (2021)

  7. Article

    Open Access

    The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments

    The mitochondrial pyruvate carrier (MPC) plays a central role in energy metabolism by transporting pyruvate across the inner mitochondrial membrane. Its heterodimeric composition and homology to SWEET and semi...

    Heike Rampelt, Iva Sucec, Beate Bersch, Patrick Horten, Inge Perschil in BMC Biology (2020)

  8. No Access

    Article

    Structure of the mitochondrial import gate reveals distinct preprotein paths

    The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins14. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex59 at 3.8-Å resolution....

    Yuhei Araiso, Akihisa Tsutsumi, Jian Qiu, Kenichiro Imai, Takuya Shiota in Nature (2019)

  9. No Access

    Article

    Mitochondrial proteins: from biogenesis to functional networks

    Mitochondria are essential for the viability of eukaryotic cells as they perform crucial functions in bioenergetics, metabolism and signalling and have been associated with numerous diseases. Recent functional...

    Nikolaus Pfanner, Bettina Warscheid in Nature Reviews Molecular Cell Biology (2019)

  10. Article

    Open Access

    Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions

    The mitochondrial contact site and cristae organizing system (MICOS) is crucial for the formation of crista junctions and mitochondrial inner membrane architecture. MICOS contains two core components. Mic10 sh...

    Manuel Hessenberger, Ralf M. Zerbes, Heike Rampelt, Séverine Kunz in Nature Communications (2017)

  11. Article

    Open Access

    Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

    The endoplasmic reticulum–mitochondria encounter structure (ERMES) connects the mitochondrial outer membrane with the ER. Multiple functions have been linked to ERMES, including maintenance of mitochondrial mo...

    Lars Ellenrieder, Łukasz Opaliński, Lars Becker, Vivien Krüger in Nature Communications (2016)

  12. Article

    Open Access

    Visualizing active membrane protein complexes by electron cryotomography

    Unravelling the structural organization of membrane protein machines in their active state and native lipid environment is a major challenge in modern cell biology research. Here we develop the STAMP (Specific...

    Vicki A.M. Gold, Raffaele Ieva, Andreas Walter, Nikolaus Pfanner in Nature Communications (2014)

  13. No Access

    Article

    Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-terminal targeting sequence

    The presequence translocase of the inner mitochondrial membrane (TIM23 complex) is essential for importing cleavable preproteins into mitochondria. The preproteins contain amino-terminal targeting sequences th...

    Raffaele Ieva, Anna K. Heißwolf, Michael Gebert, F.-Nora Vögtle in Nature Communications (2013)

  14. No Access

    Article

    Voltage-coupled conformational dynamics of mitochondrial protein-import channel

    Mitochondria contain multisubunit translocases to import preproteins from the cytosol. The presequence translocase of the inner membrane operates in a voltage-gated manner, but how a preprotein-conducting chan...

    Martin van der Laan, Sandra G Schrempp in Nature Structural & Molecular Biology (2013)

  15. No Access

    Article

    Mitochondriale Systeme für den Import von Proteinen

    Lena-Sophie Wenz, Nikolaus Pfanner, Thomas Becker in BIOspektrum (2012)

  16. No Access

    Article

    Mitochondrial protein import: from proteomics to functional mechanisms

  17. Proteomic studies revealed that mitochondria contain ∼1,000 (in yeast) to 1,500 (in humans) different proteins and led to the recent identification of new mito...

  18. Oliver Schmidt, Nikolaus Pfanner, Chris Meisinger in Nature Reviews Molecular Cell Biology (2010)

  19. No Access

    Protocol

    Native Techniques for Analysis of Mitochondrial Protein Import

    During the evolution of eukaryotic cells, the majority of mitochondrial genes have been transferred to the nuclear genome with the consequence that most mitochondrial proteins have to be imported into the orga...

    F. -Nora Vögtle, Oliver Schmidt, Agnieszka Chacinska, Nikolaus Pfanner in Protein Secretion (2010)

  20. No Access

    Article

    Motor-free mitochondrial presequence translocase drives membrane integration of preproteins

    The mitochondrial inner membrane is the central energy-converting membrane of eukaryotic cells. The electrochemical proton gradient generated by the respiratory chain drives the ATP synthase. To maintain this ...

    Martin van der Laan, Michael Meinecke, Jan Dudek, Dana P. Hutu in Nature Cell Biology (2007)

  21. No Access

    Protocol

    The Mitochondrial Machinery for Import of Precursor Proteins

    Mitochondria contain a small genome that codes for approx 1% of the total number of proteins that reside in the mitochondria. Hence, most mitochondrial proteins are encoded for by the nuclear genome. After tra...

    Kipros Gabriel, Nikolaus Pfanner in Protein Targeting Protocols (2007)

  22. No Access

    Protocol

    Isolation of Yeast Mitochondria

    Often preparations of isolated organelles contain other, unwanted, cellular components. For biochemical experiments to determine the localization of newly identified proteins, or to determine the whole set of ...

    Chris Meisinger, Nikolaus Pfanner, Kaye N. Truscott in Yeast Protocol (2006)

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