自噬
生物
细胞凋亡
半胱氨酸蛋白酶
细胞生物学
劈理(地质)
程序性细胞死亡
线粒体
细胞质
半胱氨酸蛋白酶7
生物化学
断裂(地质)
古生物学
作者
Mojgan Djavaheri‐Mergny,Maria Chiara Maiuri,Guido Kroemer
出处
期刊:Oncogene
[Springer Nature]
日期:2010-01-25
卷期号:29 (12): 1717-1719
被引量:364
摘要
Beclin 1 has a key role in the initiation of autophagy, a process of self-cannibalism in which cytoplasmic constituents are sequestered and targeted for lysosomal degradation. In a recent issue of Cell Death & Disease, Wirawan et al. report the significant finding that caspases can cleave Beclin 1, thereby destroying its pro-autophagic activity. Moreover, the C-terminal fragment of Beclin 1 that results from this cleavage acquires a new function and can amplify mitochondrion-mediated apoptosis. Of note, the BH3 domain of Beclin 1 remains within the N-terminal fragment, which has no detectable pro-apoptotic activity. These findings provide important insights into the molecular cross talk between autophagy and apoptosis.
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