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

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


  • Zha J
  • Weiler S
  • Oh KJ
  • Wei MC
  • Korsmeyer SJ


Science (New York, N.Y.)

Publication Data

December 1, 2000

Associated Grants

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

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