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- W4221036110 endingPage "101858" @default.
- W4221036110 startingPage "101858" @default.
- W4221036110 abstract "The mitochondrial permeability transition pore (PTP) is a Ca2+-dependent megachannel that plays an important role in mitochondrial physiology and cell fate. Cyclophilin D (CyPD) is a well-characterized PTP regulator, and its binding to the PTP favors pore opening. It has previously been shown that p53 physically interacts with CyPD and opens the PTP during necrosis. Accumulating studies also suggest that the F-ATP synthase contributes to the regulation and formation of the PTP. F-ATP synthase IF1 (mitochondrial ATP synthase inhibitory factor 1) is a natural inhibitor of F-ATP synthase activity; however, whether IF1 participates in the modulation of PTP opening is basically unknown. Here, we demonstrate using calcium retention capacity assay that IF1 overexpression promotes mitochondrial permeability transition via opening of the PTP. Intriguingly, we show that IF1 can interact with the p53-CyPD complex and facilitate cell death. We also demonstrate that the presence of IF1 is necessary for the formation of p53-CyPD complex. Therefore, we suggest that IF1 regulates the PTP via interaction with the p53-CyPD complex, and that IF1 is necessary for the inducing effect of p53-CyPD complex on PTP opening." @default.
- W4221036110 created "2022-04-03" @default.
- W4221036110 creator A5061109654 @default.
- W4221036110 date "2022-05-01" @default.
- W4221036110 modified "2023-09-29" @default.
- W4221036110 title "Mitochondrial ATP synthase inhibitory factor 1 interacts with the p53–cyclophilin D complex and promotes opening of the permeability transition pore" @default.
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- W4221036110 doi "https://doi.org/10.1016/j.jbc.2022.101858" @default.
- W4221036110 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35337801" @default.
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