Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis.
Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis.
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DOI：
10.1126/science.290.5497.1761
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发表时间：
2000-12
期刊：
影响因子：
56.9
通讯作者：
J. Zha;S. Weiler;K. J. Oh;M. Wei;S. Korsmeyer
中科院分区：
文献类型：
--
作者：
J. Zha;S. Weiler;K. J. Oh;M. Wei;S. Korsmeyer
许多凋亡分子在细胞凋亡过程中发生亚细胞定位。促凋亡蛋白BID进行翻译后（而不是经典的共翻译）N-豆蔻酰化时，由半胱天冬酶8切割引起暴露的甘氨酸残基。N-豆蔻酰化使BID的p7和豆蔻酰化p15片段的复合物能够靶向具有线粒体脂质组成的人工膜以及完整的线粒体。这种蛋白水解后的N-豆蔻酰化作为激活开关，增强BID诱导的细胞色素c释放和细胞死亡。
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.