Abstract
Bid is cleaved by caspase 8 during apoptosis and the truncated Bid (tBid) translocates to mitochondria by targeting cardiolipin. Amino acids 103–162 of Bid were reported as the cardiolipin-binding domain (CBD). The EGFP-CBD fusion protein targets to mitochondria and induces apoptosis. Using [3H]cardiolipin, we proved that recombinant CBD binds cardiolipin similar to tBid and tBid(G94E), a mutant with a defective BH3 domain. CBD could induce cytochrome c release from isolated mitochondria, but much less potent than tBid. Free cardiolipin inhibited the CBD-induced cytochrome c release, suggesting that it may be mediated by interfering with mitochondrial cardiolipin, especially with the interaction between cytochrome c and cardiolipin. This is consistent with the findings that CBD induced cytochrome c release in Bax-deficient cells, and that CBD suppressed mitochondrial respiration through directly interfering with cardiolipin, a critical lipid involved in oxidative phosphorylation. These results indicate the functional importance of CBD in tBid-induced apoptosis.
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Liu, J., Weiss, A., Durrant, D. et al. The cardiolipin-binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release. Apoptosis 9, 533–541 (2004). https://doi.org/10.1023/B:APPT.0000038034.16230.ea
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DOI: https://doi.org/10.1023/B:APPT.0000038034.16230.ea