The IκB Kinase Complex (IKK) Contains Two Kinase Subunits, IKKα and IKKβ, Necessary for IκB Phosphorylation and NF-κB Activation
CellPublished 1 October 1997Open access
Ebrahim Zandi, David M. Rothwarf, Mireille Delhase, Makio Hayakawa, Michael Karin
Citations1,820
SJR quartileQ1
SJR score22.61
SNIP7.62
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TL;DR
The molecular cloning and characterization of IKKbeta, a second subunit of the IKK complex, is described, which is 50% identical to IKKalpha and like it contains a kinase domain, a leucine zipper, and a helix-loop-helix.
Abstract
Recently we purified a 900 kDa cytokine-responsive IkappaB kinase complex (IKK) and molecularly cloned one of its subunits, IKKalpha, a serine kinase. We now describe the molecular cloning and characterization of IKKbeta, a second subunit of the IKK complex. IKKbeta is 50% identical to IKKalpha and like it contains a kinase domain, a leucine zipper, and a helix-loop-helix. Although IKKalpha and IKKbeta can undergo homotypic interaction, they also interact with each other and the functional IKK complex contains both subunits. The catalytic activities of both IKKalpha and IKKbeta make essential contributions to IkappaB phosphorylation and NF-kappaB activation. While the interactions between IKKalpha and IKKbeta may be mediated through their leucine zipper motifs, their helix-loop-helix motifs may be involved in interactions with essential regulatory subunits.
Keywords
Immunology and MicrobiologyMedicineBiochemistry, Genetics and Molecular Biology
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