Programmed cell death via the both intrinsic and extrinsic pathways is regulated by interactions of the Bcl-2 family protein members that determine whether the cell commits to apoptosis via mitochondrial outer membrane permeabilization (MOMP). Recently the conserved C-terminal sequences (CTSs) that mediate localization of Bcl-2 family proteins to intracellular membranes, have been shown to have additional protein-protein binding functions that contribute to the functions of these proteins in regulating MOMP. Here we review the pivotal role of CTSs in Bcl-2 family interactions including: (1) homotypic interactions between the pro-apoptotic executioner proteins that cause MOMP, (2) heterotypic interactions between pro-apoptotic and anti-apoptotic proteins that prevent MOMP, and (3) heterotypic interactions between the pro-apoptotic executioner proteins and the pro-apoptotic direct activator proteins that promote MOMP.

中文翻译：

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Bcl-2 家族蛋白的 C 端序列介导调节细胞死亡的相互作用。


通过内在和外在途径进行的程序性细胞死亡受到 Bcl-2 家族蛋白成员之间相互作用的调节，这些成员决定细胞是否通过线粒体外膜透化 (MOMP) 进行凋亡。最近，介导 Bcl-2 家族蛋白定位到细胞内膜的保守 C 端序列 (CTS) 已被证明具有额外的蛋白-蛋白结合功能，有助于这些蛋白调节 MOMP 的功能。在这里，我们回顾了 CTS 在 Bcl-2 家族相互作用中的关键作用，包括：(1) 导致 MOMP 的促凋亡刽子手蛋白之间的同型相互作用，(2) 预防 MOMP 的促凋亡和抗凋亡蛋白之间的异型相互作用， (3)促进MOMP的促凋亡刽子蛋白和促凋亡直接激活蛋白之间的异型相互作用。