Fig. 7: Graphic representation of the hypothesis explored in this work: a proof-of-concept that the loss of interaction between frataxin and mitochondrial respiratory complex I could be critical for the upstream bioenergetics’ defects in cells of patients with Friedreich ataxia. | Cell Death & Disease

Fig. 7: Graphic representation of the hypothesis explored in this work: a proof-of-concept that the loss of interaction between frataxin and mitochondrial respiratory complex I could be critical for the upstream bioenergetics’ defects in cells of patients with Friedreich ataxia.

From: Human frataxin, the Friedreich ataxia deficient protein, interacts with mitochondrial respiratory chain

Fig. 7: Graphic representation of the hypothesis explored in this work: a proof-of-concept that the loss of interaction between frataxin and mitochondrial respiratory complex I could be critical for the upstream bioenergetics’ defects in cells of patients with Friedreich ataxia.The alternative text for this image may have been generated using AI.

In healthy cells frataxin is closely attached to the mitochondrial cristae, which contain both the FeS cluster assembly machinery and the respiratory chain complexes; in FRDA cells with bioenergetics defects, perturbation of mitochondrial ultrastructure causes the mislocalization of the residual frataxin from the cristae membrane to the matrix. The enrichment of frataxin in the cristae in healthy cells makes possible its functional interaction with complex I (red box), which is lost in FRDA patients’ cells, resulting in the impairment of complex I (blue box).

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