Oligomer-based functions of mitochondrial porin

Hironori Takeda, Saori Shinoda, Chiho Goto, Akihisa Tsutsumi, Haruka Sakaue, Chunming Zhang, Takashi Hirashima, Yuta Konishi, Haruka Ono, Yu Yamamori, Kentaro Tomii, Hiroya Shiino, Yasushi Tamura, Solène Zuttion, Bruno Senger, Sylvie Friant, Hubert D. Becker, Yuhei Araiso, Nanako Kobayashi, Noriyuki Kodera, Masahide Kikkawa and Toshiya Endo ()
Additional contact information
Hironori Takeda: Kyoto Sangyo University
Saori Shinoda: Kyoto Sangyo University
Chiho Goto: Kyoto Sangyo University
Akihisa Tsutsumi: The University of Tokyo
Haruka Sakaue: Kyoto Sangyo University
Chunming Zhang: Kyoto Sangyo University
Takashi Hirashima: Kyoto Sangyo University
Yuta Konishi: Kyoto Sangyo University
Haruka Ono: Kyoto Sangyo University
Yu Yamamori: National Institute of Advanced Industrial Science and Technology (AIST)
Kentaro Tomii: National Institute of Advanced Industrial Science and Technology (AIST)
Hiroya Shiino: Yamagata University
Yasushi Tamura: Yamagata University
Solène Zuttion: UMR7156
Bruno Senger: UMR7156
Sylvie Friant: UMR7156
Hubert D. Becker: UMR7156
Yuhei Araiso: Kanazawa University
Nanako Kobayashi: Kanazawa University
Noriyuki Kodera: Kanazawa University
Masahide Kikkawa: The University of Tokyo
Toshiya Endo: Kyoto Sangyo University

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Porin, or the voltage-dependent anion channel (VDAC), is a primary β-barrel channel in the mitochondrial outer membrane. It transports small metabolites and ions through its β-barrel pore and plays key roles in apoptosis and inflammatory response. Here we report the cryo-electron microscopy structure of yeast porin (Por1) in its hexameric form at 3.2 Å resolution. This structure allows us to introduce various mutations at the protomer interfaces, uncovering three critical functions of Por1 assembly beyond transport. Por1 binds unassembled Tom22, a subunit of the mitochondrial protein import gate (the TOM complex), to facilitate protein import into the intermembrane space, maintains proper mitochondrial lipid composition in the outer membrane through lipid scramblase activity, and contributes to the retention and regulated loss of mitochondrial DNA, in cooperation with nucleases identified through screening enabled by the obtained Por1 mutant.

Date: 2025
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DOI: 10.1038/s41467-025-62021-4

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