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ID 115351
Author
Yoshinaka, Takahiro Kyushu University
Yoshizumi, Takuma Kyushu University
Furukawa, Ryo Kyushu University
Hirano, Yu National Institutes for Quantum and Radiological Science and Technology
Kuge, Osamu Kyushu University
Tamada, Taro National Institutes for Quantum and Radiological Science and Technology
Koshiba, Takumi Kyushu University|Fukuoka University
Content Type
Journal Article
Description
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, 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.
Journal Title
iScience
ISSN
25890042
Publisher
Elsevier
Volume
19
Start Page
1065
End Page
1078
Published Date
2019-09-27
Rights
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
EDB ID
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher
departments
Institute of Advanced Medical Sciences