Inhibition of NF-kappaB activation by a dominant-negative mutant of IkappaBalpha

Molecular Immunology
C G ChenM J Pearse

Abstract

The activity of the transcription factor NF-kappaB is tightly regulated by the inhibitory molecule IkappaBalpha. Upon stimulation, IkappaBalpha is rapidly degraded and NF-kappaB translocates to the nucleus to induce gene expression. The IkappaBalpha degradation is preceded by phosphorylation, suggesting that this event plays a role in the activation of NF-kappaB. In this study, we have mutated three potential phosphorylation sites in porcine IkappaBalpha and found that expression of the Ser32 mutant of IkappaBalpha (IS32A), but not Tyr42 or Ser262 mutants or wild-type IkappaBalpha, blocked the activation of NF-kappaB by TNF-alpha. These results suggest that the Ser32 residue, a potential casein kinase II phosphorylation site, is critical for NF-kappaB activation.

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Citations

Sep 11, 2007·Journal of Huazhong University of Science and Technology. Medical Sciences = Hua Zhong Ke Ji Da Xue Xue Bao. Yi Xue Ying De Wen Ban = Huazhong Keji Daxue Xuebao. Yixue Yingdewen Ban·Zhijun QuYanfeng Pan
Jun 23, 1999·Proceedings of the National Academy of Sciences of the United States of America·V T HeusslerD A Dobbelaere
Jan 13, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·Emanuela RicciottiPaola Patrignani
Oct 8, 1998·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·S C ThomasH R Wong

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