Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria.

@article{Shulga2010Sirtuin3DO,
  title={Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria.},
  author={Nataly Shulga and Robin Wilson-Smith and John G. Pastorino},
  journal={Journal of cell science},
  year={2010},
  volume={123 Pt 6},
  pages={894-902}
}
We demonstrate that the transition from a reliance on glycolysis to oxidative phosphorylation in a transformed cell line is dependent on an increase in the levels and activity of sirtuin-3. Sirtuin-3 deacetylates cyclophilin D, diminishing its peptidyl-prolyl cis-trans isomerase activity and inducing its dissociation from the adenine nucleotide translocator. Moreover, the sirtuin-3-induced inactivation of cyclophilin D causes a detachment of hexokinase II from the mitochondria that is necessary… CONTINUE READING
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