The intra-mitochondrial contact site formed by Cqd1 and the Por1-Om14 complex modulates architecture and morphology of mitochondria

• Published in: bioRxiv
• Main Authors: Khosravi, Siavash, Chelius, Xenia, Unger, Ann-Katrin, Sachsenheimer, Timo, Luechtenborg, Christian, Schieweck, Rico, Bruegger, Britta, Westermann, Benedikt, Klecker, Till, Neupert, Walter, Harner, Max E
• Format: Paper
• Language: English
• Published: Cold Spring Harbor Cold Spring Harbor Laboratory Press 09.04.2022
• Subjects: Coenzyme Q; Cytology; Cytosol; Endoplasmic reticulum; Homeostasis; Kinases; Lipid metabolism; Mitochondria; Organelles; Phospholipids; Protein kinase
• DOI: 10.1101/2022.04.09.487722

Mitochondria are essential organelles of eukaryotic cells that are characterized by their unique and complex membrane system. They are confined from the cytosol by an envelope consisting of two membranes. Signals, metabolites, proteins and lipids have to be transferred across these membranes via proteinaceous contact sites to keep mitochondria functional. In the present study we identified a novel mitochondrial contact site that is formed by Cqd1 in the inner membrane and the outer membrane complex Por1-Om14. Cqd1 is a member of the highly conserved UbiB protein kinase-like family (also called aarF domain containing kinases). It was recently shown that Cqd1 in cooperation with Cqd2 controls the cellular distribution of coenzyme Q by a yet unknown mechanism. Our data suggest that Cqd1 besides its known function in coenzyme Q homeostasis is involved in the homeostasis of phospholipids, the organization of the mitochondrial inner membrane and the interaction of mitochondria with the endoplasmic reticulum. Competing Interest Statement The authors have declared no competing interest.