A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

被引：1875

作者：

Joseph A. DiDonato ^{[2
]}

Makio Hayakawa ^{[
]}

David M. Rothwarf ^{[
]}

Ebrahim Zandi ^{[
]}

Michael Karin ^{[
]}

机构：

[1] Laboratory of Gene Regulation and Signal Transduction,Department of Pharmacology

[2] University of California at San Diego,undefined

来源：

Nature | 1997年 / 388卷 / 6642期

关键词：

D O I：

10.1038/41493

中图分类号：

学科分类号：

摘要：

Nuclear transcription factors of the NF-κB/Rel family are inhibited by IκB proteins, which inactivate NF-κB by trapping it in the cell cytoplasm. Phosphorylation of IκBs marks them out for destruction, thereby relieving their inhibitory effect on NF-κB. A cytokine-activated protein kinase complex, IKK (for IκB kinase), has now been purified that phosphorylates IκBs on the sites that trigger their degradation. A component of IKK was molecularly cloned and identified as a serine kinase. IKK turns out to be the long-sought-after protein kinase that mediates the critical regulatory step in NF-κB activation.

引用

页码：548 / 554

页数：6