Mitofilin complexes: conserved organizers of mitochondrial membrane architectureZerbes, R. M., van der Klei, I. J., Veenhuis, M., Pfanner, N., van der Laan, M. & Bohnert, M., Nov-2012, In : Biological Chemistry. 393, 11, p. 1247-1261 15 p.
Research output: Contribution to journal › Review article › Academic › peer-review
Mitofilin proteins are crucial organizers of mitochondrial architecture. They are located in the inner mitochondrial membrane and interact with several protein complexes of the outer membrane, thereby generating contact sites between the two membrane systems of mitochondria. Within the inner membrane, mitofilins are part of hetero-oligomeric protein complexes that have been termed the mitochondrial inner membrane organizing system (MINOS). MINOS integrity is required for the maintenance of the characteristic morphology of the inner mitochondrial membrane, with an inner boundary region closely apposed to the outer membrane and cristae membranes, which form large tubular invaginations that protrude into the mitochondrial matrix and harbor the enzyme complexes of the oxidative phosphorylation machinery. MINOS deficiency comes along with a loss of crista junction structures and the detachment of cristae from the inner boundary membrane. MINOS has been conserved in evolution from unicellular eukaryotes to humans, where alterations of MINOS subunits are associated with multiple pathological conditions.
|Number of pages||15|
|Publication status||Published - Nov-2012|
- cristae, crista junction, Fcj1, MINOS, Mio10, mitochondrial morphology, TRANSLOCATION CONTACT SITES, RAT-BRAIN MITOCHONDRIA, DOMINANT OPTIC ATROPHY, DYNAMIN-RELATED GTPASE, INNER-MEMBRANE, PROTEIN IMPORT, PROTEOMIC IDENTIFICATION, ELECTRON TOMOGRAPHY, CRISTAE MORPHOLOGY, OXIDATIVE STRESS