QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology

Mitochondria are the cell's power plants, and churn out molecules that provide a portable energy source throughout the cell. To do this efficiently, the mitochondria have a double membrane. The inner membrane is ruffled, which provides a large surface area for energy-producing reactions to occur on. Structures called cristae junctions and contact sites hold the folds of the inner membrane in place. As mitochondria are found in every cell in the body, mitochondrial diseases can produce a wide range of symptoms, but they commonly affect the muscles. In some forms of these diseases, the inner membrane of a mitochondrion is no longer folded; instead, the membrane may form concentric rings like the layers of an onion. Knowing how the folding of the inner membrane is regulated may therefore help scientists to better understand mitochondrial diseases. Scientists already know that several proteins join together to form a complex that anchors the mitochondrion's inner membrane to its outer membrane at cristae junctions. To learn more about the proteins involved in these complexes, Guarani et al. systematically screened for proteins that associate with cristae junctions and found a previously unknown protein called QIL1. Next, Guarani et al. conducted a series of experiments to determine what role QIL1 plays at the cristae junctions. The experiments showed that QIL1 is needed to bind a protein called MIC10 into the protein complex that anchors the cristae junctions to the outer membrane. In human and fruit fly cells without QIL1, this protein complex falls apart and is not repaired if extra MIC10 is added into the cells. Furthermore, in human cells lacking QIL1, the inner mitochondrial membrane forms the same onion-like rings seen in the cells of humans with mitochondrial diseases. Future studies are necessary to understand how the structure of the QIL1 complex is organized and to work out how the complex is capable of causing the mitochondrial inner membrane to curve.