BAP31 regulates mitochondrial function via interaction with Tom40 within ER-mitochondria contact sites.
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.
Mesh Terms:
Animals, Cell Line, Cell Line, Tumor, Cytosol, Electron Transport Complex I, Endoplasmic Reticulum, Fibroblasts, Gene Expression Regulation, HeLa Cells, Humans, Membrane Proteins, Mice, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Osteoblasts, Protein Binding, Protein Transport, Signal Transduction
Animals, Cell Line, Cell Line, Tumor, Cytosol, Electron Transport Complex I, Endoplasmic Reticulum, Fibroblasts, Gene Expression Regulation, HeLa Cells, Humans, Membrane Proteins, Mice, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Osteoblasts, Protein Binding, Protein Transport, Signal Transduction
Sci Adv
Date: Dec. 01, 2018
PubMed ID: 31206022
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