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Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis SCIENCE Zha, J. P., Weiler, S., Oh, K. J., Wei, M. C., Korsmeyer, S. J. 2000; 290 (5497): 1761-1765

Abstract

Many apoptotic molecules relocate subcellularly in cells undergoing apoptosis. The pro-apoptotic protein BID underwent posttranslational (rather than classic cotranslational) N-myristoylation when cleavage by caspase 8 caused exposure of a glycine residue. N-myristoylation enabled the targeting of a complex of p7 and myristoylated p15 fragments of BID to artificial membranes bearing the lipid composition of mitochondria, as well as to intact mitochondria. This post-proteolytic N-myristoylation serves as an activating switch, enhancing BID-induced release of cytochrome c and cell death.

View details for Web of Science ID 000165632400042

View details for PubMedID 11099414