pRB contains an E2F1-specific binding domain that allows E2F1-induced apoptosis to be regulated separately from other E2Factivities
pRB contains an E2F1-specific binding domain that allows E2F1-induced apoptosis to be regulated separately from other E2Factivities
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DOI：
10.1016/s1097-2765(03)00344-7
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发表时间：
2003-09-01
期刊：
影响因子：
16
通讯作者：
Dyson, N
中科院分区：
文献类型：
--
作者：
Dick, FA;Dyson, N
pRB和E2 F之间的相互作用对于控制细胞周期和凋亡是至关重要的。在这里，我们报告，pRB包含两个不同的E2 F结合位点。先前鉴定的pRB上的E2 F结合位点对于与DNA上的E2 F稳定缔合是必需的。第二个E2 F相互作用位点完全位于pRB的C-末端结构域内，并且对E2 F1具有特异性。通过该位点形成的E2 F1/pRB复合物对DNA具有低亲和力，但这种相互作用足以使pRB调节E2 F1诱导的细胞凋亡，并且E2 F1在DNA损伤后失去与该位点相互作用的能力。这些结果表明，pRB与个别E2 F蛋白以不同的方式相互作用，并表明，pRB的E2 F1诱导的细胞凋亡的调节是物理上分离的其他E2 F蛋白的转录控制。
The interaction between pRB and E2F is critical for control of the cell cycle and apoptosis. Here we report that pRB contains two distinct E2F binding sites. The previously identified E2F binding site on pRB is necessary for stable association with E2Fs on DNA. A second E2F interaction site is located entirely within the C-terminal domain of pRB and is specific for E2F1. E2F1/pRB complexes formed through this site have low affinity for DNA, but the interaction is sufficient for pRB to regulate E2F1-induced apoptosis, and E2F1 loses the ability to interact with this site following DNA damage. These results show that pRB interacts with individual E2F proteins in different ways and suggest that pRB's regulation of E2F1-induced apoptosis is physically separable from its transcriptional control of other E2F proteins.