Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα

被引：298

作者：

Tan, PL ^{[1
]}

Fuchs, SY ^{[1
]}

Chen, A ^{[1
]}

Wu, K ^{[1
]}

Gomez, C ^{[1
]}

Ronai, Z ^{[1
]}

Pan, ZQ ^{[1
]}

机构：

[1] CUNY Mt Sinai Sch Med, Derald H Ruttenberg Canc Ctr, New York, NY 10029 USA

来源：

MOLECULAR CELL | 1999年 / 3卷 / 04期

关键词：

D O I：

10.1016/S1097-2765(00)80481-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Activation of the transcription factor NF-kappa B in response to proinflammatory stimuli requires the phosphorylation-triggered and ubiquitin-dependent degradation of the NF-kappa B inhibitor, I kappa B alpha. Here, we show the in vitro reconstitution of the phosphorylation-dependent ubiquitination of I kappa B alpha with purified components. ROC1, a novel SCF-associated protein, is recruited by cullin 1 to form a quaternary SCFHOS-ROC1 holoenzyme (with Skp1 and the beta-TRCP homolog HOS). SCFHOS-ROC1 binds IKK beta-phosphorylated I kappa B alpha and catalyzes its ubiquitination in the presence of ubiquitin, E1, and Cdc34. ROC1 plays a unique role in the ubiquitination reaction by heterodimerizing with cullin 1 to catalyze ubiquitin polymerization.

引用

页码：527 / 533

页数：7

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