Related Experiment Video
Updated: Apr 14, 2026

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
Published on: June 16, 2023
Cox17 Protein Is an Auxiliary Factor Involved in the Control of the Mitochondrial Contact Site and Cristae Organizing
Magdalena Chojnacka1, Agnieszka Gornicka1, Silke Oeljeklaus2
1From the International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland and.
Abstract:
The mitochondrial contact site and cristae organizing system (MICOS) is a recently discovered protein complex that is crucial for establishing and maintaining the proper inner membrane architecture and contacts with the outer membrane of mitochondria. The ways in which the MICOS complex is assembled and its integrity is regulated remain elusive. Here, we report a direct link between Cox17, a protein involved in the assembly of cytochrome c oxidase, and the MICOS complex. Cox17 interacts with Mic60, thereby modulating MICOS complex integrity. This interaction does not involve Sco1, a partner of Cox17 in transferring copper ions to cytochrome c oxidase. However, the Cox17-MICOS interaction is regulated by copper ions. We propose that Cox17 is a newly identified factor involved in maintaining the architecture of the MICOS complex.
Related Concept Videos
The Inner Mitochondrial Membrane
The Supercomplexes in the Crista Membrane
Mitochondrial Protein Sorting
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Electron Transport Chain: Complex III and IV
Mitochondrial Precursor Proteins
Most of the mitochondrial...

