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    Mitochondria-endoplasmic reticulum (ER) contact sites in mammals provide platforms for various reactions, such as calcium signaling, lipid metabolism, organelle dynamics and autophagy. To fulfill these tasks, a number of proteins assemble at the contact sites including MITOL/MARCHF5, a critical mitochondrial ubiquitin ligase. How MITOL regulates mitochondrial function from the contact site, however, has been largely unresolved. Recently, a new role for MITOL in the active transport of phosphatidic acid from the ER to mitochondria was reported. In this commentary, we briefly summarize our current understanding of mitochondria-ER contact sites and discuss the recently elucidated mechanism of MITOL fine-tuning phospholipid transfer activity through ubiquitination. © The Author(s) 2023. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

    Citation

    Koji Yamano, Hiroki Kinefuchi, Waka Kojima. Mitochondrial lipid dynamics regulated by MITOL-mediated ubiquitination. Journal of biochemistry. 2024 Mar 04;175(3):217-219

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    PMID: 38156789

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