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Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis.

Science (New York, N.Y.) | Dec 1, 2000

http://www.ncbi.nlm.nih.gov/pubmed/11099414

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.

Pubmed ID: 11099414 RIS Download

Mesh terms: 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

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Associated grants

  • Agency: NCI NIH HHS, Id: CA50239-13
  • Agency: NCI NIH HHS, Id: K01 CA82231
  • Agency: NCI NIH HHS, Id: T32 CA72320-01A1

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