Article
The interaction between tBid and cardiolipin or monolysocardiolipin.
Biochemical and biophysical research communications - 13 May 2005
Liu Jihua, Durrant David, Yang Hung-Sheng, He Yongwen, Whitby Francis G, Myszka David G, Lee Ray M
Abstract excerpt
Bid, a BH3-only pro-apoptotic member of the Bcl-2 family, is cleaved by caspase 8 in apoptosis induced by death domain receptors. The carboxyl terminus of the cleavage product, tBid, remains associated with the amino terminal fragment (nBid) after cleavage. Dissociation of tBid from nBid occurs during targeting of tBid to mitochondria. We use an in vitro system and demonstrate that cardiolipin is sufficient for...
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