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Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Implications for Mitochondrial-Mediated Antiviral Innate Immunity

59 Pages Posted: 26 Feb 2019 Sneak Peek Status: Review Complete

See all articles by Takahiro Yoshinaka

Takahiro Yoshinaka

Kyushu University - Department of Biology

Hidetaka Kosako

University of Tokushima - Division of Cell Signaling

Takuma Yoshizumi

Kyushu University - Department of Biology

Ryo Furukawa

Kyushu University - Department of Biology

Yu Hirano

National Institutes for Quantum and Radiological Science and Technology - Quantum Beam Science Research Directorate

Osamu Kuge

Kyushu University - Department of Chemistry

Taro Tamada

National Institutes for Quantum and Radiological Science and Technology - Quantum Beam Science Research Directorate

Takumi Koshiba

Kyushu University - Department of Biology

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Abstract

The coiled-coil motif mediates subunit oligomerization and scaffolding, and underlies several fundamental biologic processes. Prohibitins (PHBs), mitochondrial inner membrane proteins involved in mitochondrial homeostasis and signal transduction, are predicted to have a coiled-coil motif, but their structural features are poorly understood. Here we solved the crystal structure of the heptad repeat (HR) region of PHB2 at 1.7 Å resolution. It assembles into a dimeric, antiparallel coiled-coil with a unique negatively charged area essential for the PHB interactome in mitochondria. Disruption of the HR coiled-coil prevents well-ordered PHB complexes and abolishes mitochondrial tubular networks. We found that PHB2 associated with a caseinolytic peptidase B protein homolog, also known as mitochondrial ATPase associated with diverse cellular activities ATPase chaperonin, via a coiled-coil, thereby ensuring mitochondrial-mediated antiviral innate immunity. Elucidation of the PHB complex structure in mitochondria provides insight into essential PHB interactomes required for mitochondrial dynamics as well as cellular signal transduction.

Keywords: BioID, crystal structure, homeostasis, innate immunity, interactome, mitochondrial dynamics, prohibitin, RNA virus, scaffolding, signal transduction

Suggested Citation

Yoshinaka, Takahiro and Kosako, Hidetaka and Yoshizumi, Takuma and Furukawa, Ryo and Hirano, Yu and Kuge, Osamu and Tamada, Taro and Koshiba, Takumi, Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Implications for Mitochondrial-Mediated Antiviral Innate Immunity (January 16, 2019). Available at SSRN: https://ssrn.com/abstract=3316800 or http://dx.doi.org/10.2139/ssrn.3316800
This is a paper under consideration at Cell Press and has not been peer-reviewed.

Takahiro Yoshinaka

Kyushu University - Department of Biology

Fukuoka, 819-0395
Japan

Hidetaka Kosako

University of Tokushima - Division of Cell Signaling

Tokushima, 770-8503
Japan

Takuma Yoshizumi

Kyushu University - Department of Biology

Fukuoka, 819-0395
Japan

Ryo Furukawa

Kyushu University - Department of Biology

Fukuoka, 819-0395
Japan

Yu Hirano

National Institutes for Quantum and Radiological Science and Technology - Quantum Beam Science Research Directorate

Ibaraki, 319-1106
Japan

Osamu Kuge

Kyushu University - Department of Chemistry

Fukuoka, 819-0395
Japan

Taro Tamada

National Institutes for Quantum and Radiological Science and Technology - Quantum Beam Science Research Directorate

Ibaraki, 319-1106
Japan

Takumi Koshiba (Contact Author)

Kyushu University - Department of Biology ( email )

Fukuoka, 819-0395
Japan

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