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

Joseph A. DiDonato, Makio Hayakawa, David M. Rothwarf, Ebrahim Zandi and Michael Karin ()
Additional contact information
Michael Karin: Laboratory of Gene Regulation and Signal Transduction, University of California at San Diego

Nature, 1997, vol. 388, issue 6642, 548-554

Abstract: Abstract 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.

Date: 1997
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/41493 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:388:y:1997:i:6642:d:10.1038_41493

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/41493

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().