Posttranslational N-Myristoylation of BID as a Molecular Switch for Targeting Mitochondria and Apoptosis
- 1 December 2000
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 290 (5497), 1761-1765
- https://doi.org/10.1126/science.290.5497.1761
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.Keywords
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