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    Gene. 1998 Nov 5;222(1):31-40.

    IkappaB kinase-alpha and -beta genes are coexpressed in adult and embryonic tissues but localized to different human chromosomes.

    Hu MC, Wang Y.

    Department of Cell Biology and Functional Genomics, Amgen, Inc., Thousand Oaks, CA 91320, USA. mhu@amgen.com

    Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is regulated by phosphorylation, ubiquitination, and degradation of its inhibitory factor IkappaB. Very recently, two closely related serine/threonine kinases have been identified as IkappaB kinases which are essential for IkappaB phosphorylation and NF-kappaB activation. Here, we isolated the full-length human cDNA clones encoding these two IkappaB kinases, IKK-alpha and IKK-beta. Both polypeptides contain a conserved amino-terminal kinase domain, a leucine zipper motif and a helix-loop-helix domain at their carboxyl terminus. We showed that IKK-alpha and IKK-beta were coexpressed in most human adult tissues as well as in different developmental stages of mouse embryos, suggesting that they may cooperate in the cells. The IKK-alpha and IKK-beta genes are distinct but evolutionarily conserved. Moreover, the IKK-alpha gene locus was mapped to human chromosome 10q24, whereas the IKK-beta gene locus was localized to human chromosome 8p11.2. These results indicated that both genes are not clustered on the same chromosome; nevertheless, both genes may be still regulated similarly during development and in adult tissues.

    PMID: 9813230 [PubMed - indexed for MEDLINE]

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