Cited by 3,638NF-κB Signaling PathwaysImmune Response and InflammationSignaling Pathways in Disease

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Missing Pieces in the NF-κB Puzzle

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Ghosh, Sankar, Karin, Michael·2002·Cell

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Abstract

The regulation of the transcription factor NF-kappaB activity occurs at several levels including controlled cytoplasmic-nuclear shuttling and modulation of its transcriptional activity. A critical component in NF-kappaB regulation is the IkappaB kinase (IKK) complex. This review is focused on recent progress as well as unanswered questions regarding the regulation and function of NF-kappaB and IKK.

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Crossref · 10.1016/s0092-8674(02)00703-1

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Self-citation
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Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491
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Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
Self-citation
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Self-citation
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Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
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
Self-citation
IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042
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Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872

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“This promotes the translocation of NF-κB from the cytoplasm to the nucleus driving the transcription of its target genes (47,48).”
Background
Redox signaling and histone acetylation in acute pancreatitis
Escobar, J., Pereda, J., López‐Rodas, G., & Sastre, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.009 · Cited by 84
Therapy for Chronic Obstructive Pulmonary Disease in the 21st Century
Donnelly, L., & Rogers, D. F. (2003) · Drugs · doi:10.2165/00003495-200363190-00002 · Cited by 86
Molecular mechanisms of apoptosis in the cells of the immune system in human aging
Gupta, S. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00261.x · Cited by 85
Molecular aspects of pancreatic β‐cell dysfunction: Oxidative stress, microRNA, and long noncoding RNA
Borujeni, M. J. S., Esfandiary, E., Baradaran, A., Valiani, A., Ghanadian, M., Codoñer‐Franch, P., Basirat, R., Alonso‐Iglesias, E., Mirzaei, H., & Yazdani, A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27755 · Cited by 87
“Perhaps the strongest proof for involvement of NF‐κB in IR comes from pharmacological investigations (Ghosh & Karin, 2002; Nguyen et al., 2007).”
Background
RORα is crucial for attenuated inflammatory response to maintain intestinal homeostasis
Oh, S. K., Kim, D., Kim, K., Boo, K.-J., Yu, Y. S., Kim, I. S., Jeon, Y., Im, S.-K., Lee, S.-H., Lee, J. M., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1907595116 · Cited by 84
Human Postprandial Nutrient Metabolism and Low-Grade Inflammation: A Narrative Review
Meessen, E. C. E., Warmbrunn, M. V., Nieuwdorp, M., & Soeters, M. R. (2019) · Nutrients · doi:10.3390/nu11123000 · Cited by 95
“On the other hand, cytokines, but also ROS and LPS, are acknowledged inducers of Nf-κB [82,83].”
Background
Identification of a Novel Blocker of IκBα Kinase That Enhances Cellular Apoptosis and Inhibits Cellular Invasion through Suppression of NF-κB-Regulated Gene Products
Ichikawa, H., Takada, Y., Murakami, A., & Aggarwal, B. B. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.11.7383 · Cited by 85
IκB kinase inhibitors for treating autoimmune and inflammatory disorders: potential and challenges
Strnad, J., & Burke, J. R. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.01.005 · Cited by 84
Inhibitory effects of saikosaponin-d on CCl4-induced hepatic fibrogenesis in rats
Dang, S. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i4.557 · Cited by 85
Coactivator-Associated Arginine Methyltransferase-1 Enhances Nuclear Factor-κB-Mediated Gene Transcription through Methylation of Histone H3 at Arginine 17
Miao, F., Li, S., Chavez, V., Lanting, L. L., & Natarajan, R. D. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0365 · Cited by 85
Role of extracellular superoxide in neutrophil activation: interactions between xanthine oxidase and TLR4 induce proinflammatory cytokine production
Lorne, E., Zmijewski, J. W., Zhao, X., Liu, G., Tsuruta, Y., Park, Y.-J., Dupont, H., & Abraham, E. H. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00454.2007 · Cited by 85
RETRACTED: mda-9/Syntenin Regulates the Metastatic Phenotype in Human Melanoma Cells by Activating Nuclear Factor-κB
Boukerche, H., Su, Z.-Z., Emdad, L., Sarkar, D., & Fisher, P. B. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3875 · Cited by 85
“In its classic form, NF-nB consists of homodimer or heterodimer subunits of the Rel family, including p50 and p65 subunits, which are maintained in resting cells in an inactive state in the cytoplasm through binding to InBa (19, 22 ).”
Background
Retracted
Neuroadaptations in Human Chronic Alcoholics: Dysregulation of the NF-κB System
Ökvist, A., Johansson, S., Kuzmin, A., Bazov, I., Merino-Martinez, R., Ponomarev, I., Mayfield, R. D., Harris, R. A., Sheedy, D., Garrick, T., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000930 · Cited by 84
“Phosphorylation at several sites by the IKK complex increases the DNA binding and transcriptional activities of p65 [20,51,55].”
SIRT2 regulates extracellular vesicle-mediated liver-bone communication
Lin, L., Guo, Z., He, E., Long, X., Wang, D., Zhang, Y., Guo, W., Wei, Q., He, W., Wu, W., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00803-0 · Cited by 88
Tumour necrosis factor‐α‐induced loss of intestinal barrier function requires TNFR1 and TNFR2 signalling in a mouse model of total parenteral nutrition
Feng, Y., & Teitelbaum, D. H. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.253518 · Cited by 84
“The Journal of Physiology C© 2013 The Physiological Society and the IKKγ/NEMO regulatory subunit (DiDonato et al. 1997; Rothwarf & Karin, 1999; Ghosh & Karin, 2002).”
Background
Glutamine Modulates LPS-Induced IL-8 Production through IκB/NF-κB in Human Fetal and Adult Intestinal Epithelium
Liboni, K., Li, N., Scumpia, P. O., & Neu, J. (2005) · Journal of Nutrition · doi:10.1093/jn/135.2.245 · Cited by 84
Towards subtlety: Understanding the role of Toll-like receptor signaling in susceptibility to human infections
Turvey, S. E., & Hawn, T. R. (2006) · Clinical Immunology · doi:10.1016/j.clim.2006.02.003 · Cited by 84
Control of specificity and magnitude of NF-κB and STAT1-mediated gene activation through PIASy and PIAS1 cooperation
Tahk, S., Liu, B., Chernishof, V., Wong, K. A., Wu, H., & Shuai, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701877104 · Cited by 84
TREM‐1 expression in macrophages is regulated at transcriptional level by NF‐κB and PU.1
Zeng, H., Ornatowska, M., Joo, M., & Sadikot, R. T. (2007) · European Journal of Immunology · doi:10.1002/eji.200737270 · Cited by 88
TNF-alpha Activates MUC2 Transcription via NF-kappaB but Inhibits via JNK Activation
Ahn, D. H., Crawley, S., Hokari, R., Kato, S., Yang, S. C., Li, J., & Kim, Y. (2005) · Cellular Physiology and Biochemistry · doi:10.1159/000083636 · Cited by 84
Mechanisms underlying the manipulation of host apoptotic pathways by Toxoplasma gondii
Sinai, A. P., Payne, T. M., Carmen, J. C., Hardi, L., Watson, S. J., & Molestina, R. E. (2003) · International Journal for Parasitology · doi:10.1016/j.ijpara.2003.11.009 · Cited by 84
Novel pyrazolopyrimidine derivatives targeting COXs and iNOS enzymes; design, synthesis and biological evaluation as potential anti-inflammatory agents
Abdelazeem, A. H., Abdelatef, S. A., El‐Saadi, M. T., Omar, H. A., Khan, S. I., McCurdy, C. R., & El‐Moghazy, S. M. (2014) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2014.05.025 · Cited by 84
“Furthermore, the inducible transcription factor (NF-kB) regulates the expression of several genes such as iNOS, COX-2, and TNF-a that are involved in inflammatory responses at the transcriptional level (Ghosh and Karin, 2002).”
4-Hydroxy-3-Methoxybenzoic Acid Methyl Ester: A Curcumin Derivative Targets Akt/NFκB Cell Survival Signaling Pathway: Potential for Prostate Cancer Management
Kumar, A. P., Garcia, G. E., Ghosh, R., Rajnarayanan, R. V., Alworth, W. L., & Slaga, T. J. (2003) · Neoplasia · doi:10.1016/s1476-5586(03)80057-x · Cited by 84
Ubiquitin-Regulated Recruitment of IκB Kinase ε to the MAVS Interferon Signaling Adapter
Paz, S., Vilasco, M., Arguello, M., Sun, Q., Lacoste, J., Nguyên, T. L.-A., Zhao, T., Shestakova, E. A., Zaari, S., Bibeau-Poirier, A., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00880-08 · Cited by 84
IKKβ phosphorylates p65 at S468 in transactivaton domain 2
Schwabe, R. F., & Sakurai, H. (2005) · The FASEB Journal · doi:10.1096/fj.05-3736fje · Cited by 86
“he transcription factor nuclear factor-kappa B (NF-κB) is crucially involved in the regulation of inflammation and cell death (1).”
Influential
Selective estrogen-receptor modulators suppress microglial activation and neuronal cell death via an estrogen receptor-dependent pathway
Ishihara, Y., Itoh, K., Ishida, A., & Yamazaki, T. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.10.002 · Cited by 84
“Activated IKKb phosphorylates the IkB inhibitory protein IkBa, targeting it for ubiquitination and proteasomal degradation, which allows the release of NF-kB into the nucleus, where it binds to its cognate DNA sequences to induce gene expression [32].”
Induction of a pro‐apoptotic ATM–NF‐κB pathway and its repression by ATR in response to replication stress
Wu, Z., & Miyamoto, S. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.127 · Cited by 82
“The NF-kB family of transcription factors consists of five members, RelA (p65), RelB, c-Rel, NF-kB1/p50 and NF-kB2/ p52, which exist as either homo- or heterodimers (Ghosh and Karin, 2002; Perkins, 2007).”
Role of NF-κB signaling pathway in increased tumor necrosis factor-α-induced apoptosis of lymphocytes in aged humans
Gupta, S., Bi, R.-H., Kim, C., Chiplunkar, S., Yel, L., & Gollapudi, S. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401557 · Cited by 86
Quercetin and quercitrin protect against cytokine-induced injuries in RINm5F β-cells via the mitochondrial pathway and NF-κB signaling
Dai, X., Ding, Y., Zhang, Z., Cai, X., & Li, Y. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1177 · Cited by 83
Selective Inhibition of IκB Kinase Sensitizes Mantle Cell Lymphoma B Cells to TRAIL by Decreasing Cellular FLIP Level
Roué, G., Pérez‐Galán, P., López‐Guerra, M., Villamor, N., Campo, E., & Colomer, D. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.3.1923 · Cited by 83
Beta-Catenin–NF-κB Interactions in Murine Hepatocytes: A Complex to Die for
Nejak‐Bowen, K. N., Kikuchi, A., & Monga, S. P. (2012) · Hepatology · doi:10.1002/hep.26042 · Cited by 83
Polydnavirus Ank Proteins Bind NF-κB Homodimers and Inhibit Processing of Relish
Bitra, K., Suderman, R. J., & Strand, M. R. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002722 · Cited by 83
Anti‐inflammatory effects of the genusBifidobacteriumon macrophages by modification of phospho‐IκB and SOCS gene expression
Okada, Y., Tsuzuki, Y., Hokari, R., Komoto, S., Kurihara, C., Kawaguchi, A., Nagao, S., & Miura, S. (2009) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2008.00632.x · Cited by 82
“…phosphorylation levels were determined using Western blot analysis, because gene expression of proinflammatory cytokines, including IL-1b, TNF-a and IL-12, is regulated by release of NF-jB dimers from the cytoplasmic NF-jB-IjB complex caused by the phosphorylation of IjB-a (Ghosh & Karin 2002).”
Influential
Preventive Effect of Ginkgo biloba Extract (GBB) on the Lipopolysaccharide-Induced Expressions of Inducible Nitric Oxide Synthase and Cyclooxygenase-2 via Suppression of Nuclear Factor-.KAPPA.B in RAW 264.7 Cells
Park, Y.-M., Won, J., Yun, K., Ryu, J.-H., Han, Y.-N., Choi, S.-K., & Lee, K. (2006) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.29.985 · Cited by 83
NADPH Oxidase Limits Lipopolysaccharide-Induced Lung Inflammation and Injury in Mice through Reduction-Oxidation Regulation of NF-κB Activity
Han, W., Li, H., Cai, J., Gleaves, L. A., Polosukhin, V. V., Segal, B. H., Yull, F. E., & Blackwell, T. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201809 · Cited by 84
Nuclear factor-κB activation: a molecular therapeutic target for estrogen receptor–negative and epidermal growth factor receptor family receptor–positive human breast cancer
Singh, S., Shi, Q., Bailey, S. T., Palczewski, M. J., Pardee, A. B., Iglehart, J. D., & Biswas, D. K. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0063 · Cited by 83
From molecules to neural morphology: understanding neuroinflammation in autism spectrum condition
Young, A. M. H., Chakrabarti, B., Roberts, D., Lai, M.-C., Suckling, J., & Baron-Cohen, S. (2016) · Molecular Autism · doi:10.1186/s13229-016-0068-x · Cited by 76
“These phosphorylate IκBα, leading to its polyu biquitination and degradation [43], allow NF-κB to migrate to the nucleus, where it activates the transcription of various proinflammatory genes.”

Authors: Ghosh, S., & Karin, M.
Affiliations: Howard Hughes Medical Institute (US)
University of California San Diego (US)
Corresponding author: Ghosh, Sankar
ORCID: Ghosh, Sankar
Karin, Michael
Venue: Cell
Publisher: Elsevier BV
Published: 2002-04
Volume: 109
Issue: 2
Pages: S81-S96
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(02)00703-1
OpenAlex: W1976382352
Cited by: 3,638
References: 158
Citations by year: 2026: 29 · 2025: 65 · 2024: 66 · 2023: 49 · 2022: 66 · 2021: 94 · 2020: 100 · 2019: 84 · 2018: 103 · 2017: 111 · 2016: 122 · 2015: 141 · 2014: 134 · 2013: 144 · 2012: 189
FWCI: 19.54
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4125 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: NF-κB, IκB kinase complex, transcription factor regulation, transcriptional activity, IκB, signal transduction
MeSH terms: Animals, Cell Nucleus, Cytoplasm, Enzyme Activation, Gene Expression Regulation, Humans, Signal Transduction, NF-kappa B, Protein Serine-Threonine Kinases, Catalytic Domain, Active Transport, Cell Nucleus, I-kappa B Kinase

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