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Papers In Press, published online ahead of print May 8, 2000
Protein Biochemistry, Serono Pharmaceutical Research Institute, Plan-les-Ouates, Geneva CH-1228
Corresponding Author: bruno.antonsson.ch_gva03{at}serono.com
Summary Bid is a proapoptotic, BH3-domain-only member of the Bcl-2 family. In Fas-induced apoptosis, Bid is activated through cleavage by caspase 8 into a 15.5 kDa C-terminal fragment (tcBid), and a 6.5 kDa N-terminal fragment (tnBid). Following the cleavage, tcBid translocates to the mitochondria and promotes the release of cytochrome c into the cytosol by a mechanism that is not understood. Here we report that recombinant tcBid can act as a membrane-destabilizing agent. tcBid induces destabilization and breaking of planar lipid bilayers without appearance of ionic channels; its destabilizing activity is comparable to that of Bax and at least 30-fold higher than that of full length Bid. Consistently, tcBid, but not full length Bid, permeabilizes liposomes at physiological pH. The destabilizing effect of tcBid on liposomes and planar bilayers is independent of the BH3 domain. In contrast, mutations in the BH3 domain impair tcBid ability to induce cytochrome c release from mitochondria. The permeabilizing effect of tcBid on planar bilayers, liposomes and mitochondria can be inhibited by tnBid. In conclusion, our results suggest a dual role for Bid: BH3-independent membrane destabilization and BH3-dependent interaction with other proteins. Moreover, the dissociation of Bid after cleavage by caspase 8 represents an additional step at which apoptosis may be regulated.
J. Biol. Chem, 10.1074/jbc.M003807200
Submitted on May 4, 2000
Accepted on May 8, 2000
The destabilization of lipid membranes induced by the C-terminal fragment of Caspase 8-cleaved Bid is inhibited by the N-terminal fragment
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