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Fig. 2. | Journal of Neuroinflammation

Fig. 2.

From: Mitophagy in neurological disorders

Fig. 2.

Mitophagy in neurological diseases. A The activation of mitophagy is observed in brain tissue after neurological disorders. At the same time, brain injury causes mitochondrial damage and mitochondrial dysfunction, leading to insufficient mitophagy. When mitochondria are damaged, their recyclable energy is exhausted, eventually leading to cell death. B Inhibiting mitophagy through the use of 3-MA, BNIP3-gene silencing, WNT3α, and glycine is beneficial for the protection of cranial nerves. C In contrast, Promoting mitophagy by the antagomir, rapamycin, 17-AAG, melatonin, morin, NIX, UA/AC, TFEB, PINK1, Atg1, IPC, and AMPK can protect the nervous system. D Pathogenic proteins interfere with cargo recognition, cargo loading, and autophagosome trafficking and fusion. Inadequate mitochondrial degradation is responsible for the accumulation of defective mitochondria under these conditions. Mutations in pathogenic proteins reduce mitophagy, resulting in the aggregation of defective mitochondria. The aggregated pathogenic proteins decrease autophagosomes motility in neurons. However, accumulation of pathogenic proteins (i.e., huntingtin, α-synuclein, and p-tau) is often a consequence of defective mitophagy. 3-MA, 3-methyladenine; BNIP3, B-cell lymphoma 2 kilodalton interacting protein 3; UA/AC, urolithinA/actinonin; TFEB, transcription factor EB; PINK1, PTEN-induced putative kinase 1; Atg1, autophagy-related protein; AMPK, AMP-activated protein kinase.

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