Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
复制标题
DOI：
10.1073/pnas.93.14.7063
复制
发表时间：
1996-07-09
影响因子：
11.1
通讯作者：
Reed, JC
中科院分区：
文献类型：
--
作者：
Wang, HG;Takayama, S;Reed, JC
Bcl-2蛋白通过一种未知的机制阻断程序性细胞死亡（凋亡）。以前，我们确定了Bcl-2相互作用蛋白BAG-1，增强Bcl-2的抗凋亡作用。与BAG-1一样，丝氨酸/苏氨酸蛋白激酶Raf-1也可以在功能上与Bcl-2协同抑制细胞凋亡。在这里，我们表明，Raf-1和BAG-1在体外和酵母双杂交试验中特异性相互作用。Raf-1和BAG-1也可以从哺乳动物细胞和用编码这些蛋白的重组杆状病毒感染的昆虫细胞中共免疫沉淀。此外，细菌产生的BAG-1蛋白在体外可以增加Raf-1的激酶活性，BAG-1在酵母中也激活该哺乳动物激酶。这些观察结果表明，Bcl-2结合蛋白BAG-1加入Ras和14-3-3蛋白作为激酶Raf-1的潜在激活剂。
The Bcl-2 protein blocks programmed cell death (apoptosis) through an unknown mechanism. Previously we identified a Bcl-2 interacting protein BAG-1 that enhances the anti-apoptotic effects of Bcl-2. Like BAG-1, the serine/threonine protein kinase Raf-1 also can functionally cooperate with Bcl-2 in suppressing apoptosis. Here we show that Raf-1 and BAG-1 specifically interact in vitro and in yeast two-hybrid assays. Raf-1 and BAG-1 can also be coimmunoprecipitated from mammalian cells and from insect cells infected with recombinant baculoviruses encoding these proteins. Furthermore, bacterially-produced BAG-1 protein can increase the kinase activity of Raf-1 in vitro, BAG-1 also activates this mammalian kinase in yeast. These observations suggest that the Bcl-2 binding protein BAG-1 joins Ras and 14-3-3 proteins as potential activators of the kinase Raf-1.