Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition*♦

@article{Carraro2014ChannelFB,
  title={Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition*♦},
  author={Michela Carraro and V. Giorgio and Justina {\vS}ileikytė and G. Sartori and M. Forte and G. Lippe and M. Zoratti and I. Szab{\`o} and P. Bernardi},
  journal={The Journal of Biological Chemistry},
  year={2014},
  volume={289},
  pages={15980 - 15985}
}
  • Michela Carraro, V. Giorgio, +6 authors P. Bernardi
  • Published 2014
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • Background: Whether channel formation is a general feature of F-ATP synthase dimers across species is unknown. Results: Yeast F-ATP synthase dimers form Ca2+-dependent channels, and the e and g subunits facilitate pore formation in situ through dimerization. Conclusion: F-ATP synthase dimers form the permeability transition pore of yeast. Significance: Ca2+-dependent channel formation is a conserved feature of F-ATP synthases. Purified F-ATP synthase dimers of yeast mitochondria display Ca2… CONTINUE READING
    110 Citations

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