期刊
SCIENCE
卷 290, 期 5497, 页码 1761-1765出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.290.5497.1761
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资金
- NCI NIH HHS [K01 CA82231, T32 CA72320-01A1, CA50239-13] Funding Source: Medline
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.
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