Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca 2+ -Dependent Formation of Large Channels.

Autor: Nikiforova, Anna B., Baburina, Yulia L., Borisova, Marina P., Surin, Alexey K., Kharechkina, Ekaterina S., Krestinina, Olga V., Suvorina, Maria Y., Kruglova, Svetlana A., Kruglov, Alexey G.
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Zdroj: Cells (2073-4409); Oct2023, Vol. 12 Issue 19, p2414, 19p
Abstrakt: Monomers, dimers, and individual FOF1-ATP synthase subunits are, presumably, involved in the formation of the mitochondrial permeability transition pore (PTP), whose molecular structure, however, is still unknown. We hypothesized that, during the Ca2+-dependent assembly of a PTP complex, the F-ATP synthase (subunits) recruits mitochondrial proteins that do not interact or weakly interact with the F-ATP synthase under normal conditions. Therefore, we examined whether the PTP opening in mitochondria before the separation of supercomplexes via BN-PAGE will increase the channel stability and channel-forming capacity of isolated F-ATP synthase dimers and monomers in planar lipid membranes. Additionally, we studied the specific activity and the protein composition of F-ATP synthase dimers and monomers from rat liver and heart mitochondria before and after PTP opening. Against our expectations, preliminary PTP opening dramatically suppressed the high-conductance channel activity of F-ATP synthase dimers and monomers and decreased their specific "in-gel" activity. The decline in the channel-forming activity correlated with the reduced levels of as few as two proteins in the bands: methylmalonate–semialdehyde dehydrogenase and prohibitin 2. These results indicate that proteins co-migrating with the F-ATP synthase may be important players in PTP formation and stabilization. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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