Journal
ISCIENCE
Volume 19, Issue -, Pages 1065-+Publisher
CELL PRESS
DOI: 10.1016/j.isci.2019.08.056
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Funding
- JSPS KAKENHI [17H03667, 17K19561, 18H04863]
- Takeda Science Foundation
- The Novartis Foundation (Japan) for the Promotion of Science
- Joint Usage and Joint Research Programs, the Institute of Advanced Medical Sciences, Tokushima University
- Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from AMED Grant [JP18am0101071]
- JSPS KAKENHI Grant [19H04966]
- Grants-in-Aid for Scientific Research [19H04966, 17K19561, 17H03667, 18H04863] Funding Source: KAKEN
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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-angstrom resolution, showing that 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 abolishes well-ordered PHB complexes and the mitochondrial tubular networks accompanying PHB-dependent signaling. Using a proximity-dependent biotin identification (BioID) technique in live cells, we mapped a number of mitochondrial intermembrane space proteins whose association with PHB2 relies on the HR coiled-coil region. Elucidation of the PHB complex structure in mitochondria provides insight into essential PHB interactomes required for mitochondrial dynamics as well as signal transduction.
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