Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation.

@article{Pecina2010PhosphomimeticSO,
  title={Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation.},
  author={Petr Pecina and Grigory G. Borisenko and Natalia A. Belikova and Yulia Y. Tyurina and Alena Pecinov{\'a} and Icksoo Lee and Alejandro Khalil Samhan-Arias and Karin Przyklenk and Valerian E Kagan and Maik H{\"u}ttemann},
  journal={Biochemistry},
  year={2010},
  volume={49 31},
  pages={6705-14}
}
Mammalian cytochrome c (Cytc) transfers electrons from the bc(1) complex to cytochrome c oxidase (CcO) as part of the mitochondrial electron transport chain, and it also participates in type II apoptosis. Our recent discovery of two tyrosine phosphorylation sites in Cytc, Tyr97 in bovine heart and Tyr48 in bovine liver, indicates that Cytc functions are regulated through cell signaling. To characterize the role of Cytc tyrosine phosphorylation in detail using an independent approach, we here… CONTINUE READING
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