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BAP31 regulates mitochondrial function via interaction with Tom40 within ER-mitochondria contact sites.

Sci Adv. 2019 Jun 12;5(6):eaaw1386. eCollection 2019 Jun
Takushi Namba 1
Takushi Namba 1

[No authors listed]

Author information
  • 1 Department of Marine Resource Science, Faculty of Agriculture and Marine Science, Kochi University, Nankoku 783-8502, Japan. Email: t-namba@kochi-u.ac.jp.

摘要


The endoplasmic reticulum (ER) is composed of large membrane-bound compartments, and its membrane subdomain appears to be in close contact with mitochondria via ER-mitochondria contact sites. Here, I demonstrate that the ER membrane protein, BAP31, acts as a key factor in mitochondrial homeostasis to stimulate the constitution of the mitochondrial complex I by forming an ER-mitochondria bridging protein complex. Within this complex, BAP31 interacts with mitochondria-localized proteins, including Tom40, to stimulate the translocation of NDUFS4, the component of complex I from the cytosol to the mitochondria. Disruption of the BAP31-Tom40 complex inhibits mitochondrial complex I activity and oxygen consumption by the decreased NDUFS4 localization to the mitochondria. Thus, the BAP31-Tom40 ER-mitochondria bridging complex mediates the regulation of mitochondrial function and plays a role as a previously unidentified stress sensor, representing a mechanism for the establishment of ER-mitochondria communication via contact sites between these organelles.