| Literature DB >> 9252186 |
J A DiDonato1, M Hayakawa, D M Rothwarf, E Zandi, M Karin.
Abstract
Nuclear transcription factors of the NF-kappaB/Rel family are inhibited by IkappaB proteins, which inactivate NF-kappaB by trapping it in the cell cytoplasm. Phosphorylation of IkappaBs marks them out for destruction, thereby relieving their inhibitory effect on NF-kappaB. A cytokine-activated protein kinase complex, IKK (for IkappaB kinase), has now been purified that phosphorylates IkappaBs 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-kappaB activation.Entities:
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Year: 1997 PMID: 9252186 DOI: 10.1038/41493
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962