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Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ε-dependent Apaf-1 inhibition

AuthorsElena-Real, Carlos A.; Díaz-Quintana, Antonio; González-Arzola, Katiuska ; Velázquez-Campoy, Adrián; Orzáez, Mar; López-Rivas, Abelardo ; Gil-Caballero, Sergio; Rosa, Miguel A. de la ; Díaz-Moreno, Irene
Issue Date2018
PublisherBioMed Central
CitationCell Death and Disease, 9:365 (2018)
AbstractApoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome c is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome c target. Here we explore the cytochrome c / 14-3-3ε interaction and show the ability of cytochrome c to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome c as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome c / 14-3-3ε complex. Overall, these findings suggest an additional cytochrome c-mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network.
Publisher version (URL)htpp://dx.doi.org/10.1038/s41419-018-0408-1
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