@article{oai:repo.qst.go.jp:00077112,
 author = {Yoshinaka, Takahiro and Kosako, Hidetaka and Yoshizumi, Takuma and Furukawa, Ryo and Hirano, Yuu and Kuge, Osamu and Tamada, Taro and Koshiba, Takumi and Yuu, Hirano and Taro, Tamada},
 journal = {iScience},
 month = {Sep},
 note = {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 A 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.},
 pages = {1065--1078},
 title = {Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region},
 volume = {19},
 year = {2019}
}