Lipoprotein particle formation by anti-apoptotic tBid.

The interactions of Bcl-2 family proteins with intracellular lipids are essential for the regulation of apoptosis, a mechanism of programmed cell death that is central for the health and development of multicellular organisms. Bid and its caspase-8 cleavage product, tBid, promote permeabilization of the mitochondrial outer membrane (MOM) and sequester anti-apoptotic Bcl-2 proteins to counter their cyto-protective activity. Bid and tBid also promote lipid exchange, a characteristic trait of apoptosis.

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