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Posttranslational N-Myristoylation of BID as a Molecular Switch for Targeting Mitochondria and Apoptosis

Science  01 Dec 2000:
Vol. 290, Issue 5497, pp. 1761-1765
DOI: 10.1126/science.290.5497.1761

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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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: stanley_korsmeyer{at}dfci.harvard.edu

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