T
Takashi Tatsuta
Researcher at Max Planck Society
Publications - 55
Citations - 5542
Takashi Tatsuta is an academic researcher from Max Planck Society. The author has contributed to research in topics: Mitochondrion & Intermembrane space. The author has an hindex of 34, co-authored 51 publications receiving 4873 citations. Previous affiliations of Takashi Tatsuta include Nara Institute of Science and Technology & Royal Holloway, University of London.
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Journal ArticleDOI
Quality control of mitochondria: protection against neurodegeneration and ageing
Takashi Tatsuta,Thomas Langer +1 more
TL;DR: Current knowledge on surveillance strategies that limit mitochondrial damage and ensure cellular integrity and their role in human disease are summarized.
Journal ArticleDOI
Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria
Carsten Merkwirth,Sascha Dargazanli,Takashi Tatsuta,Stefan Geimer,Beatrix Löwer,F. Thomas Wunderlich,Jiirgen-Christoph Von Kleist-Retzow,Ari Waisman,Benedikt Westermann,Thomas Langer +9 more
TL;DR: Conditional gene targeting of murine Phb2 is used to define cellular activities of prohibitins and assign an essential function for the formation of mitochondrial cristae to prohibitingins and suggest a coupling of cell proliferation to mitochondrial morphogenesis.
Journal ArticleDOI
Formation of Membrane-bound Ring Complexes by Prohibitins in Mitochondria
TL;DR: The biogenesis and structure of the prohibitin complex in Saccharomyces cerevisiae is analyzed and both Phb1 and Phb2 subunits are targeted to mitochondria by unconventional noncleavable targeting sequences at their amino terminal end.
Journal ArticleDOI
Quality Control of Mitochondrial Proteostasis
TL;DR: The central role of mitochondrial chaperones and proteases, the cytosolic ubiquitin-proteasome system, and the mitochondrial unfolded response in this interconnected quality control network is reviewed, highlighting the dual function of some proteases in protein quality control within the organelle and for the regulation of mitochondrial fusion and mitophagy.
Journal ArticleDOI
Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli.
Teru Ogura,Koichi Inoue,Takashi Tatsuta,Toshinobu Suzaki,Kiyonobu Karata,Katherine Young,Lin Hui Su,Carol A. Fierke,Jane E. Jackman,Christian R. H. Raetz,Jack Coleman,Toshifumi Tomoyasu,Hiroshi Matsuzawa +12 more
TL;DR: Pulse‐chase experiments and in vitro assays with purified components showed that FtsH, the AAA‐type membrane‐bound metalloprotease, degrades the deacetylase, which indicates that the biosynthesis of phospholipids and the lipid A moiety of lipopolysaccharide, both of which derive their fatty acyl chains from the same R‐3‐hydroxyacyl‐ACP pool, is regulated by FTSH.