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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acyltransferases / genetics
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Acyltransferases / metabolism
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Animals
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Apoptosis*
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BH3 Interacting Domain Death Agonist Protein
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Caspase 8
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Caspase 9
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Caspases / metabolism
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Cytochrome c Group / metabolism
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Humans
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Intracellular Membranes / metabolism*
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Jurkat Cells
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Liposomes / metabolism
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Mice
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Mitochondria / metabolism*
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Myristic Acid / metabolism*
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Peptide Fragments / metabolism
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Protein Conformation
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Protein Transport
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Recombinant Fusion Proteins / metabolism
Substances
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BH3 Interacting Domain Death Agonist Protein
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BID protein, human
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Bid protein, mouse
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Carrier Proteins
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Cytochrome c Group
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Liposomes
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Peptide Fragments
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Recombinant Fusion Proteins
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Myristic Acid
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Acyltransferases
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glycylpeptide N-tetradecanoyltransferase
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CASP8 protein, human
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CASP9 protein, human
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Casp8 protein, mouse
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Casp9 protein, mouse
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Caspase 8
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Caspase 9
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Caspases