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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of I_κB_α
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Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of I_κB_α

机译：泛素结合酶Ubc9 / Hus5直接参与I_κB_α的降解

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摘要

The NF-κB/Rel proteins are sequestered in the cytoplasm in association with I_κB_α. In response to external signals, I_κB_α is phosphorylated, multi-ubiquiti- nated, and degraded by proteasomes, thereby releasing NF- κB/Rel proteins to migrate to the nucleus. We have cloned a mouse ubiquitin-conjugating enzyme (mE2), which associates with I_κB_α. mE2 is homologous to the yeast Ubc9/Hus5 ubiquitin-conjugating enzyme. A transdominant-negative mu- tant of mE2 had no effect on phosphorylation of I_κB_α, but delayed its degradation. Correspondingly, tumor necrosis factor--inducible NF-κB activity was diminished. We pro- pose that mE2 is directly involved in the ubiquitin conjugation of I_κB_α, a pivotal step in its degradation pathway.
机译：NF-κB/ Rel蛋白与I_κB_α相关地被隔离在细胞质中。响应外部信号，I_κB_α被蛋白酶体磷酸化，多泛素化并降解，从而释放NF-κB/ Rel蛋白迁移至细胞核。我们克隆了与I_κB_α相关的小鼠泛素结合酶（mE2）。 mE2与酵母Ubc9 / Hus5泛素结合酶同源。 mE2的反显性突变体对I_κB_α的磷酸化没有影响，但延迟了其降解。相应地，肿瘤坏死因子诱导的NF-κB活性降低。我们提出mE2直接参与I_κB_α的泛素结合，这是其降解途径的关键步骤。

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