Kurokawa Manabu, Kornbluth Sally
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Cell. 2009 Sep 4;138(5):838-54. doi: 10.1016/j.cell.2009.08.021.
The complex process of apoptosis is orchestrated by caspases, a family of cysteine proteases with unique substrate specificities. Accumulating evidence suggests that cell death pathways are finely tuned by multiple signaling events, including direct phosphorylation of caspases, whereas kinases are often substrates of active caspases. Importantly, caspase-mediated cleavage of kinases can terminate prosurvival signaling or generate proapoptotic peptide fragments that help to execute the death program and facilitate packaging of the dying cells. Here, we review caspases as kinase substrates and kinases as caspase substrates and discuss how the balance between cell survival and cell death can be shifted through crosstalk between these two enzyme families.
凋亡的复杂过程由半胱天冬酶精心调控，半胱天冬酶是一类具有独特底物特异性的半胱氨酸蛋白酶。越来越多的证据表明，细胞死亡途径受到多种信号事件的精细调节，包括半胱天冬酶的直接磷酸化，而激酶通常是活性半胱天冬酶的底物。重要的是，半胱天冬酶介导的激酶切割可终止促生存信号或产生促凋亡肽片段，这些片段有助于执行死亡程序并促进垂死细胞的包裹。在此，我们综述了作为激酶底物的半胱天冬酶和作为半胱天冬酶底物的激酶，并讨论了如何通过这两个酶家族之间的相互作用来改变细胞生存与细胞死亡之间的平衡。
