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How the Bcl-2 family of proteins interact to regulate apoptosis

机译：Bcl-2蛋白家族如何相互作用以调节细胞凋亡

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摘要

Commitment of cells to apoptosis is governed largely by protein-protein interactions between members of the Bcl-2 protein family. Its three sub-families have distinct roles: the BH3-only proteins trigger apoptosis by binding via their BH3 domain to pro-survival relatives, while the pro-apoptotic Bax and Bak have an essential downstream role involving disruption of organellar membranes and induction of caspase activation. The BH3-only proteins act as damage sensors, held inert until their activation by stress signals. Once activated, they were thought to bind promiscuously to pro-survival protein targets but unexpected selectivity has recently emerged from analysis of their interactions. Some BH3-only proteins also bind to Bax and Bak. Whether Bax and Bak are activated directly by these BH3-only proteins, or indirectly as a consequence of BH3-only proteins neutralizing their pro-survival targets is the subject of intense debate. Regardless of this, a detailed understanding of the interactions between family members, which are often selective, has notable implications for designing anti-cancer drugs to target the Bcl-2 family.
机译：细胞对细胞凋亡的承诺主要由Bcl-2蛋白质家族成员之间的蛋白质-蛋白质相互作用决定。它的三个亚家族具有不同的作用：仅BH3蛋白通过其BH3结构域与存活亲戚结合而触发凋亡，而促凋亡的Bax和Bak具有重要的下游作用，涉及破坏细胞器膜和诱导胱天蛋白酶。激活。仅BH3蛋白质充当损伤传感器，保持惰性状态，直到它们被压力信号激活为止。一旦被激活，它们被认为与生存蛋白靶标混杂结合，但是最近通过对其相互作用的分析发现了意想不到的选择性。一些仅BH3的蛋白质也与Bax和Bak结合。 Bax和Bak是直接由这些仅BH3的蛋白激活，还是间接由于仅BH3的蛋白中和它们的生存前靶点而被激活是引起激烈争论的主题。无论如何，对家庭成员之间相互作用的详细了解（通常是选择性的）对于设计针对Bcl-2家族的抗癌药物具有显着意义。

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