Cited by 4,766NF-κB Signaling PathwaysImmune Response and InflammationSignaling Pathways in Disease

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Phosphorylation Meets Ubiquitination: The Control of NF-κB Activity

Karin, Michael, Ben-Neriah, Yinon·2000·Annual Review of Immunology

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Abstract

NF-kappaB (nuclear factor-kappaB) is a collective name for inducible dimeric transcription factors composed of members of the Rel family of DNA-binding proteins that recognize a common sequence motif. NF-kappaB is found in essentially all cell types and is involved in activation of an exceptionally large number of genes in response to infections, inflammation, and other stressful situations requiring rapid reprogramming of gene expression. NF-kappaB is normally sequestered in the cytoplasm of nonstimulated cells and consequently must be translocated into the nucleus to function. The subcellular location of NF-kappaB is controlled by a family of inhibitory proteins, IkappaBs, which bind NF-kappaB and mask its nuclear localization signal, thereby preventing nuclear uptake. Exposure of cells to a variety of extracellular stimuli leads to the rapid phosphorylation, ubiquitination, and ultimately proteolytic degradation of IkappaB, which frees NF-kappaB to translocate to the nucleus where it regulates gene transcription. NF-kappaB activation represents a paradigm for controlling the function of a regulatory protein via ubiquitination-dependent proteolysis, as an integral part of a phosphorylationbased signaling cascade. Recently, considerable progress has been made in understanding the details of the signaling pathways that regulate NF-kappaB activity, particularly those responding to the proinflammatory cytokines tumor necrosis factor-alpha and interleukin-1. The multisubunit Ika…

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PA-X protein of H5N1 avian influenza virus inhibits NF-kappaB activity, a potential mechanism for PA-X counteracting the host innate immune responses
Hu, J., Kong, M., Cui, Z., Gao, Z., Ma, C., Hu, Z., Jiao, X., & Liu, X. (2020) · Veterinary Microbiology · doi:10.1016/j.vetmic.2020.108838 · Cited by 17
Anti-inflammatory activity of Jatropha curcas L. in brain glial cells primary cultures
Bastos, E. M. S., da Silva, A. B., Coelho, P. L. C., Borges, J. M. P., da Silva, V. D. A., Moreau, V. H., & Costa, S. L. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113201 · Cited by 15
An immunomodulatory polysaccharide from blackberry seeds and its action on RAW 264.7 cells via activation of NF-κB/MAPK pathways
Wang, J., Zhang, H., Wang, H., Wang, J., Sun‐Waterhouse, D., Waterhouse, G. I. N., Ma, C., & Kang, W. (2020) · Food and Agricultural Immunology · doi:10.1080/09540105.2020.1747407 · Cited by 16
“Previous studies have shown that the phosphorylation of I κ B α (the main inhibitor of NF-κ B) could be enhanced by plant polysaccharides, causing rapid degradation of I κ B protease (Ghosh & Hayden, 2008; Karin & Ben-Neriah, 2000).”
Dehydrodiconiferyl alcohol from Silybum marianum (L.) Gaertn accelerates wound healing via inactivating NF-κB pathways in macrophages
Hu, X., Qin, N., Xue, J., Li, S., Huang, X., Sun, J., Xu, F., Li, Z., Li, D., & Hua, H. (2019) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13205 · Cited by 18
Adipokine zinc-α2-glycoprotein alleviates lipopolysaccharide-induced inflammatory responses through the β3-AR/PKA/CREB pathway.
Guo, J., Li, Y., Zhao, R.-Q., & Yang, X.-J. (2019) · Cytokine · doi:10.1016/j.cyto.2019.154742 · Cited by 14
Labdanes and megastigmanes from Vitex negundo var. heterophylla.
Xu, J., Hu, B., Yuan, L., Wu, Y., Luan, S., Yuan, T., Wang, D., & Chen, L.-X. (2019) · Fitoterapia · doi:10.1016/j.fitote.2019.104265 · Cited by 14
Protium javanicum Burm. Methanol Extract Attenuates LPS-Induced Inflammatory Activities in Macrophage-Like RAW264.7 Cells
Ahujaa, A., Kim, M.-Y., & Cho, J. (2019) · Evidence-Based Complementary and Alternative Medicine · doi:10.1155/2019/2910278 · Cited by 14
“Signals from external stimuli are translocated through adaptor molecules, which activate the IκB kinase (IKK) complex and phosphorylates cytosolic IκB, followed by ubiquitination and sequential activationNFκB into the nucleus, and culminating in proinflammatory cytokine activation (for example, iNOS/NO, COX-2, and TNF…”
BackgroundInfluential
Scientific validation of anti-arthritic effect of Kashayams – A polyherbal formulation in collagen induced arthritic rats
S., A. I., Krishnan, S., Peter, J., Sabu, V., & Helen, A. (2019) · Journal of Ayurveda and Integrative Medicine · doi:10.1016/j.jaim.2018.02.139 · Cited by 14
“It is then translocated from the cytoplasm into the nucleus to mediate transcription of proinflammatory cytokines [11] including inducible enzymes cyclooxygenase (COX-2) and inducible nitric oxide synthase (iNOS).”
Background
IDH2 Deficiency Aggravates Fructose-Induced NAFLD by Modulating Hepatic Fatty Acid Metabolism and Activating Inflammatory Signaling in Female Mice
Pan, J., Kim, H.-S., Beane, K., Montalbano, A. M., Lee, J., Kim, Y. J., Kim, J. H., Kong, B. C., Kim, S., Park, J.-W., et al. (2018) · Nutrients · doi:10.3390/nu10060679 · Cited by 14
“Since IL-1β is directly related with transactivation of NF-κB p65 [18], we further measured the phosphorylation of”
Method
Z-ligustilide and anti-inflammatory prostaglandins have common biological properties in macrophages and leukocytes
Schwager, J., Gagno, L., Richard, N., Simon, W., Weber, P., & Bendik, I. (2018) · Nutrition and Metabolism · doi:10.1186/s12986-018-0239-1 · Cited by 14
“[46], even minor shifts in the amount, cellular localization or association of NF-κB elements drastically influence the outcome of the response.”
Background
Extracts of Porphyra tenera (Nori Seaweed) Activate the Immune Response in Mouse RAW264.7 Macrophages via NF-κB Signaling
Song, J.-H., Kang, H.-B., Park, S.-H., Jeong, J.-H., Park, J., You, Y., Lee, Y.-H., Lee, J., Kim, E., Choi, K.-C., et al. (2017) · Journal of Medicinal Food · doi:10.1089/jmf.2017.4014 · Cited by 14
High Expression of FGD3, a Putative Regulator of Cell Morphology and Motility, Is Prognostic of Favorable Outcome in Multiple Cancers
Willis, S., Sun, Y.-L., Abramovitz, M., Fei, T., Young, B., Lin, X.-Q., Ni, M., Achua, J., Regan, M., Gray, K., et al. (2017) · JCO Precision Oncology · doi:10.1200/po.17.00009 · Cited by 14
“Through a highly conserved recognized destructionmotif (DSGIDS) in bothFGD3andFGD1as well as in other unrelated proteins including IkBs and b-catenin, downregulation occurs through the ubiquitin/proteasome system via phosphorylation by GSK-3b of the serine residues in the DSGIDS motif.(33) Thus, both FGD3 and FGD1 int…”
Background
Agomelatine, a MT1/MT2 melatonergic receptor agonist with serotonin 5-HT2C receptor antagonistic properties, suppresses Prevotella intermedia lipopolysaccharide-induced production of proinflammatory mediators in murine macrophages.
Hyeon, J., Choi, E., Choe, S., Park, H., Choi, J., Choi, I., & Kim, S.-J. (2017) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2017.05.015 · Cited by 14
Fuzheng Huayu Formula (扶正化瘀方) prevents rat renal interstitial fibrosis induced by HgCl2 via antioxidative stress and down-regulation of nuclear factor-kappa B activity
Yuan, J.-L., Tao, Y.-Y., Wang, Q.-L., Shen, L., & Liu, C.-H. (2017) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-016-2540-z · Cited by 14
Baicalin Down-Regulates IL-1β-Stimulated Extracellular Matrix Production in Nasal Fibroblasts
Shin, J.-M., Kang, J.-H., Lee, S., Park, I., & Lee, H.-M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168195 · Cited by 14
Ferritinophagy in inflammatory and autoimmune diseases: Mechanistic insights and therapeutic potentials
Wang, Y. Q., Li, Y., Jiang, J., Hong, Y., Gao, S., & Hua, C. (2025) · Autoimmunity Reviews · doi:10.1016/j.autrev.2025.103954 · Cited by 15
The role of ankyrin repeat-containing proteins in epigenetic and transcriptional regulation
Wu, M., Zhao, Y., Yang, J., Yang, F., Dai, Y., Wang, Q., Chen, C., & Chu, X. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02519-4 · Cited by 16
Clinical and preclinical studies of mesenchymal stem cells to alleviate peritoneal fibrosis
Zheng, L., Chen, W.-M., Yao, K.-J., Xie, Y.-N., Liao, C., & Zhou, T.-B. (2024) · Stem cell research & therapeutics · doi:10.1186/s13287-024-03849-3 · Cited by 13
“The most powerful activators of NF-κB are inflammatory cytokines like tumor necrosis factor (TNF) or interleukin-1 (IL-1), as well as pathogen-derived molecules that trigger Toll-like receptors (TLRs) such as lipopolysaccharide (LPS), viral, and bacterial DNA and RNA [47, 50].”
Background
Quercetin attenuates inflammation in rosacea by directly targeting p65 and ICAM-1
Meng, X., Li, Y., Wang, F., Li, T., Wang, B., Wang, Q., Long, J., Xie, H., Zhang, Y., & Li, J. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122675 · Cited by 12
Hexafluoropropylene oxide trimer acid exposure triggers necroptosis and inflammation through the Wnt/β-catenin/NF-κB axis in the liver
Zhang, X., Li, B., Huo, S., Du, J., Zhang, J., Song, M., Shao, B., & Li, Y. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.167033 · Cited by 10
Role of Orai‐family channels in the activation and regulation of transcriptional activity
Nieto‐Felipe, J., Macias‐Díaz, A., Sánchez-Collado, J., Berna‐Erro, A., Jardín, I., Salido, G. M., López, J. J., & Rosado, J. A. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30971 · Cited by 15
Suppressive Effects of Isofraxidin on Depressive-like Behaviors Induced by Chronic Unpredictable Mild Stress in Mice
Wu, X., Gu, J., Zou, Z., Yu, M., Zhang, C., Xiao, Q., Chen, X., & Li, C. (2022) · Brain Sciences · doi:10.3390/brainsci12101376 · Cited by 13
Organic UV Filters Induce Toll-like-Receptors and Related Signaling Pathways in Peripheral Blood Mononuclear Cells of Juvenile Loggerhead Sea Turtles (Caretta caretta)
Cocci, P., Mosconi, G., & Palermo, F. (2022) · Animals · doi:10.3390/ani12050594 · Cited by 13
“It has been demonstrated that NF-κB activation requires initiating phosphorylation of IκBα [47].”
Background
Decrease in MAP3Ks expression enhances the cell death caused by hyperthermia
Enomoto, A., Fukasawa, T., Terunuma, H., Nakagawa, K., Yoshizaki, A., Sato, S., & Miyagawa, K. (2022) · International Journal of Hyperthermia · doi:10.1080/02656736.2021.2024281 · Cited by 13
Farrerol ameliorate adjuvant-induced ankle injury via alteration of PPAR-γ signal pathway.
Tian, Z., Zhang, H.-X., & Shang, C. (2021) · Journal of food biochemistry · doi:10.1111/jfbc.13585 · Cited by 13
New insights into molecular mechanisms of “Cold or Hot” nature of food: When East meets West
Zhou, Y., & Xu, B. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110361 · Cited by 15
Zanthoxylum zanthoxyloides inhibits lipopolysaccharide- and synthetic hemozoin-induced neuroinflammation in BV-2 microglia: roles of NF-κB transcription factor and NLRP3 inflammasome activation
Ogunrinade, F., Guetchueng, S. T., Katola, F. O., Aderogba, M. A., Akande, I., Sarker, S. D., & Olajide, O. A. (2020) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgaa019 · Cited by 18
Design and pharmaceutical applications of proteolysis-targeting chimeric molecules
Liang, Y., Nandakumar, K. S., & Cheng, K. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114211 · Cited by 16
Maturation of the Acute Hepatic TLR4/NF-κB Mediated Innate Immune Response Is p65 Dependent in Mice
Zarate, M., Nguyen, L. M., Dios, R. K. D., Zheng, L.-J., & Wright, C. J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01892 · Cited by 13
“Hepatic NF-κB p65 Subunit Gene and Protein Expression Is Developmentally Regulated The transcription factor NF-κB has been reported to have a central role in the regulation of the innate immune response (43, 44).”
Background
NF-κB p50-deficient immature myeloid cell (p50-IMC) adoptive transfer slows the growth of murine prostate and pancreatic ductal carcinoma
Suresh, R., Barakat, D. J., Barberi, T., Zheng, L., Jaffee, E., Pienta, K., & Friedman, A. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2019-000244 · Cited by 13
Pin1 Plays Essential Roles in NASH Development by Modulating Multiple Target Proteins
Inoue, M.-K., Nakatsu, Y., Yamamotoya, T., Hasei, S., Kanamoto, M., Naitou, M., Matsunaga, Y., Sakoda, H., Fujishiro, M., Ono, H., et al. (2019) · Cells · doi:10.3390/cells8121545 · Cited by 16
“The detachment of IκBα induces the nuclear translocation of RelA/p50 heterodimers and initiates the induction of various proinflammatory genes [71].”
Background
Tissue-type plasminogen activator selectively inhibits multiple toll-like receptors in CSF-1-differentiated macrophages
Das, L., Azmoon, P., Banki, M. A., Mantuano, E., & Gonias, S. (2019) · PLoS ONE · doi:10.1371/journal.pone.0224738 · Cited by 13
“IκBα binds NFκB in the cytoplasm and prevents NFκB translocation into the nucleus [30, 31].”
Background
Prevention of calpain-dependent degradation of STK38 by MEKK2-mediated phosphorylation
Enomoto, A., Fukasawa, T., Tsumoto, H., Karube, M., Nakagawa, K., Yoshizaki, A., Sato, S., Miura, Y., & Miyagawa, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-52435-8 · Cited by 15
TRUSS Exacerbates NAFLD Development by Promoting IκBα Degradation in Mice
Yu, C., Wang, Q., Wu, M., Song, B., Chen, L., Lou, J., Tang, L., Yu, X., Niu, N., Yang, X., et al. (2018) · Hepatology · doi:10.1002/hep.30066 · Cited by 15
“IκBα degradation is triggered by direct phosphorylation by the IKK complex at two critical serine residues, Ser32 and Ser36.(32,33) Because phosphorylation of IKKβ or IκBα (Fig.”
Background
Epigenetic and non-epigenetic functions of the RYBP protein in development and disease.
da Silva, C. J. S., Simón, R., & Busturia, A. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.03.011 · Cited by 13
Suppression of inflammation by the rhizome of Anemarrhena asphodeloides via regulation of nuclear factor-κB and p38 signal transduction pathways in macrophages
Kim, B. R., Cho, Y.-C., Le, H. T. T., Vuong, H. L., Lee, S., & Cho, S. (2017) · Biomedical Reports · doi:10.3892/br.2017.895 · Cited by 13
“NF-κB is a pivotal regulator of inflammation that controls expression of proinflammatory genes (5).”
Background
Tumor Necrosis Factor α Induces the Expression of the Endothelial Cell-Specific Receptor Roundabout4 through the Nuclear Factor-κB Pathway.
Tanaka, T., Maekawa, N., Kashio, T., Izawa, K., Ishiba, R., Shirakura, K., Ishimoto, K., Hino, N., Aird, W., Doi, T., et al. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b16-00938 · Cited by 13
Inhibitory effects of 3α-hydroxy-lup-20(29)-en-23, 28-dioic acid on lipopolysaccharide-induced TNF-α, IL-1β, and the high mobility group box 1 release in macrophages
Liu, X., Zou, Q.-P., Huang, J., Yook, C., Whang, W. K., Lee, H., & Kwon, O. (2017) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2017.1301803 · Cited by 16
Double phosphorylation‐induced structural changes in the signal‐receiving domain of IκBα in complex with NF‐κB
Yazdi, S., Naumann, M., & Stein, M. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25181 · Cited by 12
A20 Haploinsufficiency Aggravates Transplant Arteriosclerosis in Mouse Vascular Allografts: Implications for Clinical Transplantation
Moll, H., Lee, A., Peterson, C. R., Cervantes, J. R., Wojcik, B. M., Parulkar, A., Mele, A., LoGerfo, P. J., Siracuse, J., Csizmadia, E., et al. (2016) · Transplantation · doi:10.1097/tp.0000000000001407 · Cited by 13
“Phosphorylation of Ser-32 of IκBα and Ser-536 of p65 are surrogatemarkers of the activation status of these proteins.(19) Similarly, mRNA levels of NF-κB–dependent VCAM-1 and ICAM-1, 2 molecules that enable vascular adhesion and transmigration of mononuclear cells that are a major source of proinflammatory cytokines,(…”
Background
KPNA2 Silencing, Regulated by E3 Ubiquitin Ligase FBXW7, Alleviates Endothelial Dysfunction and Inflammation Through Inhibiting the Nuclear Translocation of p65 and IRF3: A Possible Therapeutic Approach for Atherosclerosis
Xing, Z., Zhen, Y., Chen, J., Du, M., Li, D., Liu, R., & Zheng, J. (2023) · Inflammation · doi:10.1007/s10753-023-01863-w · Cited by 12
Research progress on the role of FGF21 in insulin resistance
Zhang, H., Zhu, R., Sun, Q., & Du, L. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1619462 · Cited by 10
“This dissociation leads to the ubiquitination and degradation of I k B, facilitating the translocation of NF-k B into the nucleus, where it binds to the k B site in the promoter region to activate target genes (107).”
African swine fever virus I177L induces host inflammatory responses by facilitating the TRAF6-TAK1 axis and NLRP3 inflammasome assembly
Wu, P.-X., Yang, W.-P., Feng, T., Zhang, J., Zhu, G.-L., Du, X.-G., Ru, Y., Zhao, Y.-F., Wu, S., Li, D., et al. (2025) · Journal of Virology · doi:10.1128/jvi.02080-24 · Cited by 12
Pterostilbene protects against lipopolysaccharide-induced inflammation and blood–brain barrier disruption in immortalized brain endothelial cell lines in vitro
Zhou, Y., Yang, Y., Tian, R., & Wai, S.-C.-A. (2025) · Scientific Reports · doi:10.1038/s41598-025-85144-6 · Cited by 12
ATG5 attenuates inflammatory signaling in mouse embryonic stem cells to control differentiation
Li, S., Sun, J., Zhang, B.-W., Yang, L., Wan, Y.-C., Chen, B., Xu, N., Xu, Q., Fan, J., Shang, J.-N., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.01.026 · Cited by 16
Cell-Penetrating Peptide Conjugated Au Nanoclusters Selectively Suppress Refractory Lymphoma Cells via Targeting Both Canonical and Noncanonical NF-κB Signaling Pathways.
Lai, J., Yao, Y., Zhang, Y.-L., Liu, Y., Lu, C., Meng, C., Xia, D., Li, Y., Cao, K., Gao, X.-Y., et al. (2022) · Bioconjugate chemistry · doi:10.1021/acs.bioconjchem.2c00529 · Cited by 12
Bovine delta papillomavirus E5 oncoprotein negatively regulates the cGAS-STING signaling pathway in cattle in a spontaneous model of viral disease
Falco, F. D., Cutarelli, A., Cătoi, A. F., Uberti, B. Ď., Cuccaro, B., & Roperto, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.937736 · Cited by 14
Verapamil attenuates oxidative stress and inﬂammatory responses in cigarette smoke (CS)-induced murine models of acute lung injury and CSE-stimulated RAW 264.7 macrophages via inhibiting the NF-κB pathway.
Wu, X.-M., Hussain, M., Syed, S. K., Saadullah, M., Alqahtani, A., Alqahtani, T., Aldahish, A., Fatima, M., Shaukat, S., Hussain, L., et al. (2022) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2022.112783 · Cited by 12
Retracted
Protective Effect of Nigella sativa and Onion Extract against 5-Fluorouracil-Induced Hepatic Toxicity
Zaki, S. M., & Waggas, D. (2021) · Nutrition and Cancer · doi:10.1080/01635581.2021.2019794 · Cited by 12
Chronic Mild Stress and Venlafaxine Treatment Were Associated with Altered Expression Level and Methylation Status of New Candidate Inflammatory Genes in PBMCs and Brain Structures of Wistar Rats
Białek, K. I., Czarny, P. L., Wigner, P., Synowiec, E., Barszczewska-Pietraszek, G., Bijak, M., Szemraj, J., Niemczyk, M., Tota-Glowczyk, K., Papp, M., et al. (2021) · Genes · doi:10.3390/genes12050667 · Cited by 14
In silico evaluation of the antidiabetic activity of natural compounds from Hovenia dulcis Thunberg
de Godoi, R. S., Almerão, M., & da Silva, F. D. (2020) · Journal of Herbal Medicine · doi:10.1016/j.hermed.2020.100349 · Cited by 12
8-bromo-7-methoxychrysin targets NF-κB and FoxM1 to inhibit lung cancer stem cells induced by pro-inflammatory factors
Yuan, Q., Wen, M., Xu, C., Chen, A., Qiu, Y., Cao, J., Zhang, J., & Song, Z. (2019) · Journal of Cancer · doi:10.7150/jca.30143 · Cited by 12
“It is well known that NF-κB plays a significant role in many signaling pathways including those that are involved in cancer development and progression [37].”
Background
Retracted
Role of GluN2A NMDA receptor in homocysteine-induced prostaglandin E2 release from neurons
Rajagopal, S., Fitzgerald, A., Deep, S., Paul, S., & Poddar, R. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14775 · Cited by 12
“To clarify the role NFjB in homocysteine-GluN2A NMDAR induced activation of the COX2/PGE2 signaling pathway and the role of MAPKs in this process, we next evaluated the effect of homocysteine on IB degradation, a seminal step in NF-B activation (Karin and Ben-Neriah 2000).”
Background
Understanding the implications of engineered nanoparticle induced autophagy in human epidermal keratinocytes in vitro
Gautam, A., Rakshit, M., Nguyen, K., Kathawala, M. H., Nguyen, L. T. H., Tay, C. Y., Wong, E., & Ng, K. (2019) · NanoImpact · doi:10.1016/j.impact.2019.100177 · Cited by 12
Chemical modulation of transcription factors
Wiedemann, B. M., Weisner, J., & Rauh, D. (2018) · MedChemComm · doi:10.1039/c8md00273h · Cited by 12
Atomic force microscopy technique used for assessment of the anti-arthritic effect of licochalcone A via suppressing NF-κB activation.
Yang, F., Su, X.-H., Pi, J., Liao, K.-S., Zhou, H., Sun, Y., Liu, J., Guo, X., Jiang, J.-H., Jin, H., et al. (2018) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2018.04.142 · Cited by 12
Non-muscular myosin light chain kinase triggers intermittent hypoxia-induced interleukin-6 release, endothelial dysfunction and permeability
Recoquillon, S., Gómez-Guzmán, M., Rodier, M., Koffi, C., Nitiéma, M., Gagnadoux, F., Martínez, M. C., & Andriantsitohaina, R. (2017) · Scientific Reports · doi:10.1038/s41598-017-13268-5 · Cited by 12
Dexamethasone promotes regeneration of crushed inferior alveolar nerve by inhibiting NF-κB activation in adult rats.
Gao, W., Tong, D.-D., Li, Q., Huang, P., & Zhang, F.-H. (2017) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2017.03.025 · Cited by 12
Manatee invariants reveal functional pathways in signaling networks
Amstein, L., Ackermann, J., Scheidel, J., Fulda, S., Dikič, I., & Koch, I. (2017) · BMC Systems Biology · doi:10.1186/s12918-017-0448-7 · Cited by 12
Vinexin β Ablation Inhibits Atherosclerosis in Apolipoprotein E–Deficient Mice by Inactivating the Akt–Nuclear Factor κB Inflammatory Axis
Guan, H.-J., Cheng, W.-L., Guo, J., Chao, M., Zhang, Y., Gong, J., Zhu, X.-Y., She, Z.-G., Huang, Z., & Li, H.-L. (2017) · Journal of the American Heart Association : Cardiovascular and Cerebrovascular Disease · doi:10.1161/jaha.116.004585 · Cited by 12
“IjBa phosphorylation via IKKb results in IjBa degradation and NF-jB release.(44) IKKb is a crucial component of the IKK-signalosome, which facilitates NF-jB activation in response to most inflammatory stimuli.”
Background
Natural Compounds for Wound Healing
Georgescu, M., Marinaș, I. C., Popa, M., Stan, T. R., Lazăr, V., Bertesteanu, S. V., & Chifiriuc, M. C. (2016) · InTech eBooks · doi:10.5772/65652 · Cited by 19
“The inhibition of NFkB is generally considered a useful strategy in the treatment of inflammatory disturbances [51], this pathway being an important and attractive therapeutic target.”
The cGAS-STING signaling pathway in the regulation of pulmonary infections: a systematic review
Xu, Q., & Zhu, J. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1628481 · Cited by 11
Role and mechanisms of cuproptosis in the pathogenesis of Wilson's disease (Review)
Chen, H., Wang, X., Jin, X., Pu, Y., Ye, H., Ma, Y., & Zhang, J. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5558 · Cited by 15
Ameliorative Effect of Ginsenoside Rc on 5-Fluorouracil-Induced Chemotherapeutic Intestinal Mucositis via the PI3K-AKT/NF-κB Signaling Pathway: In Vivo and In Vitro Evaluations
Xu, L., Zhao, X., Tang, F., Zhang, J., Peng, C. Y., & Ao, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313085 · Cited by 11
Salvianolic acid B in fibrosis treatment: a comprehensive review
Liang, Q., Liu, X., Peng, X., Luo, T., Su, Y. R., Xu, X., Xie, H., Gao, H. C., Chen, Z., & Xie, C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1442181 · Cited by 13
NFκB signalling in colorectal cancer: Examining the central dogma of IKKα and IKKβ signalling
McKenzie, M., Lian, G., Pennel, K. A. F., Quinn, J. A., Jamieson, N. B., & Edwards, J. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e32904 · Cited by 11
Breaking Down Barriers: Epithelial Contributors to Monogenic IBD Pathogenesis
Ouahed, J., Griffith, A. E., Collen, L. V., & Snapper, S. B. (2024) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izad319 · Cited by 18
Co-Stimulation of AGEs and LPS Induces Inflammatory Mediators through PLCγ1/JNK/NF-κB Pathway in MC3T3-E1 Cells
Tanabe, N., Tomita, K., Manaka, S., Ichikawa, R., Takayama, T., Kawato, T., Ono, M., Masai, Y., Utsu, A., Suzuki, N., et al. (2023) · Cells · doi:10.3390/cells12101383 · Cited by 11
“NF-κB p50 and p65 are composed of heterodimers and have an inhibitory protein, IκB, in the cytoplasm [29,30].”
Background
Targeting neddylation as a novel approach to lung cancer treatment (Review)
Tian, Z.-L., Li, J., Ma, R.-J., Li, T., Sun, Z., & Huang, S.-H. (2023) · International Journal of Oncology · doi:10.3892/ijo.2023.5513 · Cited by 11
“Thus, NF‐κB is usually present in the cytoplasm in an inactive form (43).”
BackgroundInfluential
MicroRNA‑143‑3p levels are reduced in the peripheral blood of patients with gestational diabetes mellitus and influences pancreatic β‑cell function and viability
Liu, C., Feng, H., Zhang, L., Guo, Y., Ma, J., & Yang, L. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11780 · Cited by 9
“This activated NF‐κB then promotes the transcription of genes associated with path‐ ways controlling inflammatory responses, cell proliferation and apoptosis, impairing β‐cell survival and function (55).”
The dual role of the CD95 and CD95L signaling pathway in glioblastoma
Zhang, Y., Jin, T., Dou, Z., Wei, B., Zhang, B., & Sun, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1029737 · Cited by 14
AMPK/Sirt1-mediated inflammation is positively correlated with myocardial fibrosis during ageing
Song, Y., Zhang, Y., Zhang, X., Hu, S., Wang, J., Deng, G., & Zhou, Z. (2022) · Acta cardiologica. Supplementum · doi:10.1080/00015385.2022.2119667 · Cited by 10
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“14,15 In addition, I kappa B kinase (IKK) induced phosphorylation of I j B, which promotes I j B degradation and release, ﬁnally leading to activation of NF-j B. 16,17 IKK/NF-j B pathway exerts antiapoptosis function through many other proteins, such as Bcl-2.”

Authors: Karin, M., & Ben-Neriah, Y.
Affiliations: Hebrew University of Jerusalem (IL)
Department of Pharmacology, Laboratory of Gene Regulation and Signal Transduction University of California, San Diego, La Jolla, California, 92093-0636;
ORCID: Karin, Michael
Venue: Annual Review of Immunology
Publisher: Annual Reviews
Published: 2000-04
Volume: 18
Issue: 1
Pages: 621-663
ISSN: 0732-0582 (ISSN-L)
1545-3278
DOI: 10.1146/annurev.immunol.18.1.621
OpenAlex: W2147921405
Cited by: 4,766
References: 243
Citations by year: 2026: 78 · 2025: 109 · 2024: 86 · 2023: 101 · 2022: 114 · 2021: 112 · 2020: 129 · 2019: 114 · 2018: 129 · 2017: 153 · 2016: 156 · 2015: 135 · 2014: 186 · 2013: 201 · 2012: 194
FWCI: 22.12
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01 CA76188, R01CA076188)
National Institute of Allergy and Infectious Diseases (R01AI043477, R01 AI43477)
National Institute of Environmental Health Sciences (R37ES004151, R37 ES04151)
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 phosphorylation, ubiquitination, IκB kinase, IKKα, IKKβ, E3 ubiquitin ligase, proteolysis, NF-κB nuclear translocation, TNF signaling, IL-1 signaling, Rel family transcription factors, inflammation, transcriptional regulation
MeSH terms: NF-KappaB Inhibitor alpha, Amino Acid Sequence, Animals, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phosphorylation, Transcription Factors, Ubiquitins, Signal Transduction, Down-Regulation, NF-kappa B, Protein Serine-Threonine Kinases, I-kappa B Proteins, I-kappa B Kinase, NF-kappa B p50 Subunit

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Phosphorylation Meets Ubiquitination: The Control of NF-κB Activity

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