Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
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DOI：
10.1128/mcb.20.3.929-935.2000
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发表时间：
2000-02-01
影响因子：
5.3
通讯作者：
Martinou, JC
中科院分区：
文献类型：
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作者：
Eskes, R;Desagher, S;Martinou, JC
在许多类型的细胞凋亡中，促凋亡蛋白Bax在线粒体水平上经历构象变化。该事件总是先于线粒体细胞色素c的释放，其在胞质溶胶中通过与Apaf-1结合来激活半胱天冬酶。Bax触发细胞色素c释放的机制尚不清楚。在这里，我们表明，BH 3结构域仅促凋亡蛋白Bid结合后，Bax寡聚化，然后整合在线粒体外膜，在那里它触发细胞色素c释放。Bid引发的Bax线粒体膜插入可能是导致细胞凋亡的途径中的关键步骤。
In many types of apoptosis, the proapoptotic protein Bax undergoes a change in conformation at the level of the mitochondria. This event always precedes the release of mitochondrial cytochrome c, which, in the cytosol, activates caspases through binding to Apaf-1. The mechanisms by which Bax triggers cytochrome c release are unknown. Here we show that following binding to the BH3-domain-only proapoptotic protein Bid, Bax oligomerizes and then integrates in the outer mitochondrial membrane, where it triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis.