Coupling of Mitochondrial Import and Export Translocases by Receptor-Mediated Supercomplex Formation
Jian Qiu,Lena-Sophie Wenz,Ralf M. Zerbes,Silke Oeljeklaus,Maria Bohnert,David A. Stroud,Christophe Wirth,Lars Ellenrieder,Nicolas Thornton,Stephan Kutik,Sebastian Wiese,Agnes Schulze-Specking,Nicole Zufall,Agnieszka Chacinska,Bernard Guiard,Carola Hunte,Bettina Warscheid,Martin van der Laan,Nikolaus Pfanner,Nils Wiedemann,Thomas Becker +20 more
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TLDR
It is shown that the cytosolic domain of Tom22 links TOM and SAM into a supercomplex, facilitating precursor transfer on the intermembrane space side, and reveals receptor-mediated coupling of import and export translocases as a means of precursor channeling.About:
This article is published in Cell.The article was published on 2013-08-01 and is currently open access. It has received 112 citations till now. The article focuses on the topics: Sorting and assembly machinery & Translocase of the outer membrane.read more
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Journal ArticleDOI
Mitochondrial Machineries for Protein Import and Assembly.
Nils Wiedemann,Nikolaus Pfanner +1 more
TL;DR: The versatility and dynamic organization of the mitochondrial protein import machineries are discussed, which are crucial for understanding the integration of protein translocases into a large network that controls organelle biogenesis, function, and dynamics.
Journal ArticleDOI
Mitochondrial proteins: from biogenesis to functional networks
TL;DR: How the mitochondrial protein import machinery functions as a key organizer of these protein networks, its involvement in the formation of membrane contact sites, and how defects in protein import can lead to disease are discussed.
Journal ArticleDOI
The Protein Import Machinery of Mitochondria—A Regulatory Hub in Metabolism, Stress, and Disease
Angelika B. Harbauer,René P. Zahedi,Albert Sickmann,Albert Sickmann,Nikolaus Pfanner,Chris Meisinger +5 more
TL;DR: The protein import activity can function as a sensor of mitochondrial fitness and provides a direct means of regulating biogenesis, composition, and turnover of the organelle.
Journal ArticleDOI
Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.
Dennis Gessmann,Yong Hee Chung,Emily J. Danoff,Ashlee M. Plummer,Clifford W. Sandlin,Nathan R. Zaccai,Karen G. Fleming +6 more
TL;DR: The results suggest that OMP assembly machineries are required in vivo to enable physical control over the spontaneously occurring OMP folding reaction in the periplasm, and propose BamA does so by creating bilayer defects, which are known to accelerate the intrinsic folding reaction.
Journal ArticleDOI
Molecular architecture of the active mitochondrial protein gate
Takuya Shiota,Takuya Shiota,Kenichiro Imai,Jian Qiu,Victoria L. Hewitt,Kher Shing Tan,Hsin-Hui Shen,Noriyuki Sakiyama,Yoshinori Fukasawa,Sikander Hayat,Megumi Kamiya,Arne Elofsson,Kentaro Tomii,Paul Horton,Nils Wiedemann,Nikolaus Pfanner,Trevor Lithgow,Toshiya Endo,Toshiya Endo +18 more
TL;DR: A biochemical analysis reveals how the main protein entry gate of mitochondria imports preproteins and mapped the active translocator down to single amino acid residues, revealing different transport paths for pre Proteins through the Tom40 channel.
References
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