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In mammals, the intrinsic pathway of apoptosis, or programmed cell death (PCD), mainly involves activation of the apoptosome-dependent caspase cascade upon binding of cytochrome c to Apaf-1 in the cytoplasm. 1 In plants, however, cytochrome c is likewise released from the mitochondria upon death stimuli, 2 , 3 but nothing is known on its cytoplasmic function or targets. Actually, the function of cytochrome c is still controversial as it is mostly immobilized (ca. 90%) in the mitochondrial cristae under homeostatic conditions – and, therefore, it is unable to have any role as redox carrier 4 – but is massively liberated into the cytoplasm and even the nucleus under PCD conditions.
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Martínez‐Fábregas et al. (2014) studied this question.
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