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首页> 外文期刊>Molecular and Cellular Biology >The signal response of IkappaB alpha is regulated by transferable N- and C-terminal domains.
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The signal response of IkappaB alpha is regulated by transferable N- and C-terminal domains.

机译：IkappaB alpha的信号响应受可转移的N和C末端域调节。

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摘要

IkappaB alpha retains the transcription factor NF-kappaB in the cytoplasm, thus inhibiting its function. Various stimuli inactivate IkappaB alpha by triggering phosphorylation of the N-terminal residues Ser32 and Ser36. Phosphorylation of both serines is demonstrated directly by phosphopeptide mapping utilizing calpain protease, which cuts approximately 60 residues from the N terminus, and by analysis of mutants lacking one or both serine residues. Phosphorylation is followed by rapid proteolysis, and the liberated NF-kappaB translocates to the nucleus, where it activates transcription of its target genes. Transfer of the N-terminal domain of IkappaB alpha to the ankyrin domain of the related oncoprotein Bcl-3 or to the unrelated protein glutathione S-transferase confers signal-induced phosphorylation on the resulting chimeric proteins. If the C-terminal domain of IkappaB alpha is transferred as well, the resulting chimeras exhibit both signal-induced phosphorylation and rapid proteolysis. Thus, the signal response of IkappaB alpha is controlled by transferable N-terminal and C-terminal domains.
机译：IkappaB alpha在细胞质中保留了转录因子NF-kappaB，因此抑制了其功能。各种刺激通过触发N端残基Ser32和Ser36的磷酸化使IkappaBα失活。这两种丝氨酸的磷酸化直接通过钙蛋白酶蛋白酶通过磷酸肽作图来证明，该蛋白酶从N末端切下约60个残基，并通过分析缺少一个或两个丝氨酸残基的突变体来证明。磷酸化后迅速进行蛋白水解，释放的NF-κB易位至细胞核，从而激活其靶基因的转录。 IkappaBα的N末端结构域转移到相关癌蛋白Bcl-3的锚蛋白结构域或转移到无关蛋白质谷胱甘肽S-转移酶上，从而使信号诱导的嵌合蛋白磷酸化。如果IkappaBα的C末端域也被转移，则所得的嵌合体既显示信号诱导的磷酸化作用，又显示快速的蛋白水解作用。因此，IkappaB alpha的信号响应受可转移的N端和C端域控制。

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