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IκB Kinase-β: NF-κB Activation and Complex Formation with IκB Kinase-α and NIK
Abstract
Activation of the transcription factor nuclear factor kappa B (NF-κB) by inflammatory cytokines requires the successive action of NF-κB–inducing kinase (NIK) and IκB kinase–α (IKK-α). A widely expressed protein kinase was identified that is 52 percent identical to IKK-α. IκB kinase–β (IKK-β) activated NF-κB when overexpressed and phosphorylated serine residues 32 and 36 of IκB-α and serines 19 and 23 of IκB-β. The activity of IKK-β was stimulated by tumor necrosis factor and interleukin-1 treatment. IKK-α and IKK-β formed heterodimers that interacted with NIK. Overexpression of a catalytically inactive form of IKK-β blocked cytokine-induced NF-κB activation. Thus, an active IκB kinase complex may require three distinct protein kinases.
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Citations
Cites
Function and Activation of NF-kappaB in the Immune System
Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125
TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182
Self-citation
Cited by
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,494
Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842
Missing Pieces in the NF-κB Puzzle
Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638
NF-κB activation by tumour necrosis factor requires the Akt serine–threonine kinase
Nidai Ozes, O., Mayo, L. D., Gustin, J. A., Pfeffer, S. R., Pfeffer, L. M., & Donner, D. B. (1999) · Nature · doi:10.1038/43466 · Cited by 1,832
NF-κB, the first quarter-century: remarkable progress and outstanding questions
Hayden, M. S., & Ghosh, S. (2012) · Genes & Development · doi:10.1101/gad.183434.111 · Cited by 1,693
NF-κB in the liver—linking injury, fibrosis and hepatocellular carcinoma
Luedde, T., & Schwabe, R. F. (2011) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.213 · Cited by 1,345
Dandona, P., Aljada, A., Chaudhuri, A., Mohanty, P., & Garg, R. (2005) · Circulation · doi:10.1161/01.cir.0000158483.13093.9d · Cited by 1,263
The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal
Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102
Annunziata, C. M., Davis, R. E., Demchenko, Y., Bellamy, W., Gabrea, A., Zhan, F., Lenz, G., Hanamura, I., Wright, G., Xiao, W., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.07.004 · Cited by 952
Molecular basis of the effects of shear stress on vascular endothelial cells
Li, Y.-S. J., Haga, J. H., & Chien, S. (2005) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2004.09.030 · Cited by 904
Citric acid cycle intermediates as ligands for orphan G-protein-coupled receptors
He, W., Miao, F. J.-P., Lin, D. C.-H., Schwandner, R. T., Wang, Z., Gao, J., Chen, J.-L., Tian, H., & Ling, L. (2004) · Nature · doi:10.1038/nature02488 · Cited by 909
McKay, L. I., & Cidlowski, J. A. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.4.0375 · Cited by 805
Inhibiting NF-κB activation by small molecules as a therapeutic strategy
Gupta, S. C., Sundaram, C., Reuter, S., & Aggarwal, B. B. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.05.004 · Cited by 762
Human toll-like receptor 2 confers responsiveness to bacterial lipopolysaccharide
Kirschning, C. J., Wesche, H., Merrill Ayres, T., & Rothe, M. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.11.2091 · Cited by 753
Self-citationNod1, an Apaf-1-like Activator of Caspase-9 and Nuclear Factor-κB
Inohara, N., Koseki, T., del Peso, L., Hu, Y., Yee, C., Chen, S., Carrio, R., Merino, J., Liu, D., Ni, J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14560 · Cited by 742
Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674
Recent advances torwards understanding redox mechanisms in the activation of nuclear factor κb
Janssen-Heininger, Y. M. W., Poynter, M. E., & Baeuerle, P. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00218-5 · Cited by 666
The IκB kinase complex in NF‐κB regulation and beyond
Hinz, M., & Scheidereit, C. (2014) · The EMBO Reports · doi:10.1002/embr.201337983 · Cited by 572
Nissen, R. M., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.827900 · Cited by 559
Staudt, L. M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000109 · Cited by 485
Severe liver degeneration and lack of NF-κ B activation in NEMO/IKKγ-deficient mice
Rudolph, D., Yeh, W.-C., Wakeham, A., Rudolph, B., Nallainathan, D., Potter, J., Elia, A. J., & Mak, T. W. (2000) · Genes & Development · doi:10.1101/gad.14.7.854 · Cited by 479
Inflammatory Pathways in Liver Homeostasis and Liver Injury
Tacke, F., Luedde, T., & Trautwein, C. (2009) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-008-8091-0 · Cited by 393
Schwandner, R., Yamaguchi, K., & Cao, Z. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.7.1233 · Cited by 349
Self-citationLi, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219
Anderson, H. D. I., Rahmutula, D., & Gardner, D. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309552200 · Cited by 186
Xu, X., Sun, Y., Cen, X., Shan, B., Zhao, Q., Xie, T., Wang, Z., Hou, T., Xue, Y., Zhang, M., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00858-3 · Cited by 171
Act1, a negative regulator in CD40- and BAFF-mediated B cell survival
Qian, Y., Qin, J., Cui, G., Naramura, M., Snow, E. C., Ware, C. F., Fairchild, R. L., Omori, S. A., Rickert, R. C., Scott, M., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.09.001 · Cited by 143
Sylla, B. S., Hung, S. C., Davidson, D. M., Hatzivassiliou, E., Malinin, N. L., Wallach, D., Gilmore, T. D., Kieff, E., & Mosialos, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10106 · Cited by 137
Structural studies of NF-κB signaling
Zheng, C., Yin, Q., & Wu, H. (2011) · Cell Research · doi:10.1038/cr.2010.171 · Cited by 134
The role of NF-κB/IκB proteins in cancer: implications for novel treatment strategies
Schwartz, S. A., Hernandez, A., & Mark Evers, B. (1999) · Surgical Oncology · doi:10.1016/s0960-7404(00)00012-8 · Cited by 132
Anandamide Inhibits Nuclear Factor-κB Activation through a Cannabinoid Receptor-Independent Pathway
Sancho, R., Calzado, M. A., Di Marzo, V., Appendino, G., & Muñoz, E. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.2.429 · Cited by 120
Qin, J., Jiang, Z., Qian, Y., Casanova, J.-L., & Li, X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400785200 · Cited by 110
NEMO Trimerizes through Its Coiled-coil C-terminal Domain
Agou, F., Ye, F., Goffinont, S., Courtois, G., Yamaoka, S., Israël, A., & Véron, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201964200 · Cited by 79
Hamilton, M. J., Caswell, R. C., Canham, N., Cole, T., Firth, H. V., Foulds, N., Heimdal, K., Hobson, E., Houge, G., Joss, S., et al. (2018) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2017-104620 · Cited by 43
Sun, W., Wang, H., Zhao, X., Yu, Y., Fan, Y., Wang, H., Wang, X., Lu, X., Zhang, G., Fu, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.104224 · Cited by 20
Metadata
- Authors
- Woronicz, J. D., Gao, X., Cao, Z., Rothe, M., & Goeddel, D. V.
- Venue
- Science
- Published
- 1997-10-31
- Volume
- 278
- Issue
- 5339
- Pages
- 866-870
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1997509253
- Cited by
- 1,181
- References
- 3
- FWCI
- 56.41
- Type
- journal article
- Language
- en
- Open access
- closed
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