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Inhibition of NF-κB Activity by IκBβ in Association with κB-Ras

机译：IκBβ与κB-Ras结合抑制NF-κB活性

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IκBβ, one of the major IκB proteins, is only partially degraded in response to most extracellular signals. However, the molecular mechanism of this event is unknown. We show here that IκBβ exists in at least two different forms: one that is bound to the NF-κB dimer and the other bound to both NF-κB and κB-Ras, a Ras-like small G protein. Removal of cellular κB-Ras enhances whereas excess κB-Ras blocks induced IκBβ degradation. Remarkably, κB-Ras functions in both GDP- and GTP-bound states, and mutations of the conserved guanine-binding residues of κB-Ras abrogate its ability to block degradation of IκBβ. κB-Ras also directly blocks the in vitro phosphorylation of IκBβ by IKKβ. These observations suggest that IκBβ in the ternary complex is resistant to degradation by most signals. We suggest that specific signals, in addition to those that activate only IKK, are essential for the complete degradation of IκBβ.
机译：IκBβ是主要的IκB蛋白之一，仅响应大多数细胞外信号而部分降解。但是，此事件的分子机制尚不清楚。我们在这里显示IκBβ至少以两种不同形式存在：一种与NF-κB二聚体结合，另一种与NF-κB和κB-Ras（一种类似Ras的小G蛋白）结合。细胞κB-Ras的去除增强，而过量的κB-Ras阻止诱导的IκBβ降解。值得注意的是，κB-Ras在GDP和GTP结合状态下均起作用，并且κB-Ras保守的鸟嘌呤结合残基的突变消除了其阻止IκBβ降解的能力。 κB-Ras也直接阻断了IKKβ的IκBβ的体外磷酸化。这些观察结果表明三元复合物中的IκBβ能够抵抗大多数信号的降解。我们建议，除了仅激活IKK的信号外，特定信号对于IκBβ的完全降解至关重要。

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