Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis.
Journal:
Science 2000 DecAuthors:
Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ
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 s
...[more]erves as an activating switch, enhancing BID-induced release of cytochrome c and cell death.[less]
Mesh Headings:
Acyltransferases, Animals, Apoptosis, BH3 Interacting Domain Death Agonist Protein, Carrier Proteins, Caspase 8, Caspase 9, Caspases, Cytochrome c Group, Humans, Intracellular Membranes, Jurkat Cells, Liposomes, Mice, Mitochondria, Myristic Acid, Peptide Fragments, Protein Conformation, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein Transport, Recombinant Fusion Proteins