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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BackgroundInfluential
A Sulfated Polysaccharide from Saccharina japonica Suppresses LPS-Induced Inflammation Both in a Macrophage Cell Model via Blocking MAPK/NF-κB Signal Pathways In Vitro and a Zebrafish Model of Embryos and Larvae In Vivo
Wang, S., Ni, L., Fu, X., Duan, D., Xu, J., & Gao, X. (2020) · Marine Drugs · doi:10.3390/md18120593 · Cited by 52
Andrographolide attenuates microglia-mediated Aβ neurotoxicity partially through inhibiting NF-κB and JNK MAPK signaling pathway
Yang, R., Liu, S., Zhou, J., Bu, S.-H., & Zhang, J. (2017) · Immunopharmacology and immunotoxicology · doi:10.1080/08923973.2017.1344989 · Cited by 50
“ANDRO reduced the mRNA levels of TNF-a, IL-1b, COX-2, and iNOS in ab (1-42)-stimulated microglial cells”
Background
Inhibition of atherogenesis by the COP9 signalosome subunit 5 in vivo
Asare, Y., Ommer-Bläsius, M., Azombo, F. A., Alampour‐Rajabi, S., Sternkopf, M., Sanati, M., Gijbels, M. J., Schmitz, C., Sinitski, D., Tilstam, P. V., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618411114 · Cited by 56
Baicalein inhibits TNF-α-induced NF-κB activation and expression of NF-κB-regulated target gene products.
Li, J.-B., Ma, J., Wang, K.-S., Mi, C., Wang, Z., Piao, L.-X., Xu, G., Li, X., Lee, J., & Jin, X.-J. (2016) · Oncology Report · doi:10.3892/or.2016.5108 · Cited by 50
Nuclear factor kappa B expression in non-small cell lung cancer
Zhang, L., Ludden, C. M., Cullen, A. J., Tew, K. D., de Barros, A. L. B., & Townsend, D. M. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115459 · Cited by 50
“Instead, the C-terminal domains of p50 and p52 contain 6– 7 ankyrin repeats responsible for sequestration in the cytosol, a characteristic particular to NF-kB inhibitory proteins (IkB) [19].”
Background
Nuclear factor kappa B activation appears weaker in schizophrenia patients with high brain cytokines than in non-schizophrenic controls with high brain cytokines
Murphy, C., Lawther, A. J., Webster, M., Asai, M., Kondo, Y., Matsumoto, M., Walker, A., & Weickert, C. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01890-6 · Cited by 49
Molecular mechanisms of action of naringenin in chronic airway diseases.
Chin, L.-H., Hon, C.-M., Chellappan, D., Chellian, J., Madheswaran, T., Zeeshan, F., Awasthi, R., Aljabali, A. A. A., Tambuwala, M., Dureja, H., et al. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173139 · Cited by 49
Wnt-Induced Stabilization of KDM4C Is Required for Wnt/β-Catenin Target Gene Expression and Glioblastoma Tumorigenesis
Chen, Y., Fang, R., Yue, C., Chang, G., Li, P., Guo, Q., Wang, J., Zhou, A., Zhang, S., Fuller, G. N., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1229 · Cited by 69
“It is known that β-TrCP interacts with the DS(PO4)GXXS(PO4) degron of substrates (35).”
Background
Progesterone inhibits inflammatory response in E.coli- or LPS-Stimulated bovine endometrial epithelial cells by NF-κB and MAPK pathways
Cui, L., Wang, H., Lin, J., Wang, Y., Dong, J., Li, J., & Li, J. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.103568 · Cited by 60
Targeting IκappaB kinases for cancer therapy
Awasthee, N., Rai, V., Chava, S. P., Nallasamy, P., Kunnumakkara, A. B., Bishayee, A., Chauhan, S. C., Challagundla, K. B., & Gupta, S. C. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.02.007 · Cited by 53
“IκBα phosphorylation triggers the polyubiquitination (by E2- and E3-ligases) and subsequent degradation (by 26S proteasome) of IκBα [19].”
Background
Chelidonine inhibits TNF‐α‐induced inflammation by suppressing the NF‐κB pathways in HCT116 cells
Zhang, Z. H., Mi, C., Wang, K.-S., Wang, Z., Li, M. Y., Zuo, H.-X., Xu, G., Li, X., Piao, L.-X., Ma, J., et al. (2018) · Phytotherapy Research · doi:10.1002/ptr.5948 · Cited by 49
“All members of the NF‐κB family harbor an N‐terminal Rel homology domain that is responsible for DNA binding, dimerization, and association with inhibitory proteins known as IκBs (Ghosh, May, Chelidonine; cIAP‐1, cellular enase‐2; FLIP, cellular FLICE a; IL‐8, interleukin 8; iNOS, yte chemotactic protein 1; lear facto…”
Background
NKILA inhibits NF-κB signaling and suppresses tumor metastasis
Ke, S., Li, R.-C., Meng, F.-K., & Fang, M.-H. (2018) · Aging · doi:10.18632/aging.101359 · Cited by 49
Paeoniflorin Ameliorates Experimental Autoimmune Encephalomyelitis via Inhibition of Dendritic Cell Function and Th17 Cell Differentiation
Zhang, H., Qi, Y., Yuan, Y., Cai, L., Xu, H., Zhang, L., Su, B., & Nie, H. (2017) · Scientific Reports · doi:10.1038/srep41887 · Cited by 48
Interplay between proteasome inhibitors and NF-κB pathway in leukemia and lymphoma: a comprehensive review on challenges ahead of proteasome inhibitors
Pakjoo, M., Ahmadi, S. E., Zahedi, M., Jaafari, N., Khademi, R., Amini, A., & Safa, M. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01433-5 · Cited by 54
“Phosphorylation of IκB proteins by the IKK complex (IKKα, IKKβ, and IKKγ) activates NF-κB [24, 70].”
Background
Polysaccharide from Potentilla anserina L ameliorate pulmonary edema induced by hypobaric hypoxia in rats
Shi, J., Liu, Z., Li, M., Guo, J. Z., Chen, L., Ding, L., Ding, X., Zhou, T., & Zhang, J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111669 · Cited by 48
Tumor-associated macrophages regulate gastric cancer cell invasion and metastasis through TGFβ2/NF-κB/Kindlin-2 axis
Wang, Z., Yang, Y., Cui, Y.-C., Wang, C., Lai, Z., Li, Y.-S., Zhang, W., Mustonen, H., Puolakkainen, P., Ye, Y.-J., et al. (2020) · Chinese journal of cancer research = Chung-kuo yen cheng yen chiu · doi:10.21147/j.issn.1000-9604.2020.01.09 · Cited by 48
An Overview of Novel Dietary Supplements and Food Ingredients in Patients with Metabolic Syndrome and Non-Alcoholic Fatty Liver Disease
Figueiredo, P. S., Inada, A. C., Fernandes, M. R., Arakaki, D. G., Freitas, K. D. C., Guimarães, R. D. C. A., do Nascimento, V. A., & Hiane, P. A. (2018) · Molecules · doi:10.3390/molecules23040877 · Cited by 48
Melatonin potentiates the antitumor effect of curcumin by inhibiting IKKβ/NF-κB/COX-2 signaling pathway
Shrestha, S., Zhu, J., Wang, Q., Du, X., Liu, F., Jiang, J., Song, J., Xing, J., Sun, D., Hou, Q., et al. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4097 · Cited by 52
“Phosphorylated I κ B proteins subsequently undergo proteasome-mediated degradation, thereby liberating free NF-κ B p65/p50 dimers to translocate to the nucleus that can then modulate gene transcription (41).”
TMEM43-S358L mutation enhances NF-κB-TGFβ signal cascade in arrhythmogenic right ventricular dysplasia/cardiomyopathy
Zheng, G., Jiang, C., Li, Y., Yang, D., Ma, Y., Zhang, B., Li, X., Zhang, P., Hu, X., Zhao, X., et al. (2019) · Protein & Cell · doi:10.1007/s13238-018-0563-2 · Cited by 48
The Recent Research Progress of NF-κB Signaling on the Proliferation, Migration, Invasion, Immune Escape and Drug Resistance of Glioblastoma
Shi, P., Xu, J., & Cui, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210337 · Cited by 52
Hazelnut protein-derived peptide LDAPGHR shows anti-inflammatory activity on LPS-induced RAW264.7 macrophage
Ren, D.-Y., Wang, P., Liu, C.-L., Wang, J., Liu, X.-Q., Liu, J.-S., & Min, W.-H. (2018) · Journal of Functional Foods · doi:10.1016/j.jff.2018.04.024 · Cited by 47
Synbiotics containing sea buckthorn polysaccharides ameliorate DSS-induced colitis in mice via regulating Th17/Treg homeostasis through intestinal microbiota and their production of BA metabolites and SCFAs
Yuan, M., Chang, L., Gao, P., Li, J., Xin-yuan, L., Hua, M., Li, X., Liu, X., & Lan, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133794 · Cited by 50
Palmitoylethanolamide Modulation of Microglia Activation: Characterization of Mechanisms of Action and Implication for Its Neuroprotective Effects
D’Aloia, A., Molteni, L., Gullo, F., Bresciani, E., Artusa, V., Rizzi, L., Ceriani, M., Meanti, R., Lecchi, M., Coco, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063054 · Cited by 48
“The “canonical” pathway is triggered by microbial products and proinflammatory cytokines such as TNF-α and IL-1, usually leading to activation of RelA- or cRel-containing complexes [22].”
Background
Sodium butyrate reduces bovine mammary epithelial cell inflammatory responses induced by exogenous lipopolysaccharide, by inactivating NF-κB signaling
Sun, X., Luo, S., Jiang, C., Tang, Y., Cao, Z., Jia, H., Xu, Q., Zhao, C., Loor, J. J., & Xu, C. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18189 · Cited by 47
“A variety of extracellular stimuli lead to the rapid phosphorylation, ubiquitination, and ultimately proteolytic degradation of IκBα, which frees NF-κB to translocate to the nucleus, where it regulates transcription of tumor necrosis factor α (TNFA), interleukin-6 (IL6), and interleukin-1B (IL1B; Karin and Ben-Neriah,…”
Background
In vitro and in vivo anti-inflammatory effects of different extracts from Epigynum auritum through down-regulation of NF-κB and MAPK signaling pathways
Yang, M., Wang, Y., Patel, G., Xue, Q., Njateng, G. S. S., Cai, S., Cheng, G., & Kai, G. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113105 · Cited by 56
High Risk of Hepatocellular Carcinoma Development in Fibrotic Liver: Role of the Hippo-YAP/TAZ Signaling Pathway
Moon, H., Cho, K., Shin, S., Kim, D. Y., Han, K., & Ro, S. W. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030581 · Cited by 56
“The most potent activators of NF-kB include inflammatory cytokines such as TNF-α or IL-1, as well as Toll-like receptors (TLRs) [68,69], which can also trigger cell proliferative signals through NF-Kb [70,71].”
Background
Aqueous synthesized quantum dots interfere with the NF-κB pathway and confer anti-tumor, anti-viral and anti-inflammatory effects.
Hu, Z.-L., Song, B., Xu, L., Zhong, Y.-L., Peng, F., Ji, X.-Y., Zhu, F., Yang, C., Zhou, J.-Y., Su, Y.-Y., et al. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.08.047 · Cited by 46
“Phosphorylated IkB is degraded via a proteasome-mediated pathway, and NF-kB dimers are then released and translocate to the nucleus to activate gene transcription [8].”
Background
NADPH Oxidase 4 (NOX4) in Cancer: Linking Redox Signals to Oncogenic Metabolic Adaptation
Szántó, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052702 · Cited by 52
MicroRNA-182 improves spinal cord injury in mice by modulating apoptosis and the inflammatory response via IKKβ/NF-κB
Fei, M., Li, Z., Cao, Y.-W., Jiang, C., Lin, H.-D., & Chen, Z.-X. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00606-5 · Cited by 45
“In the IKK complex, the catalytic subunit IKKβ has an important role in the phosphorylation of the IκB protein [10].”
Background
Neferine alleviates memory and cognitive dysfunction in diabetic mice through modulation of the NLRP3 inflammasome pathway and alleviation of endoplasmic-reticulum stress
Wu, X., Deng, M., Gao, Z., Dang, Y., Li, Y., & Li, C. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106559 · Cited by 52
Evaluation of artesunate for the treatment of adult T-cell leukemia/lymphoma.
Ishikawa, C., Senba, M., & Mori, N. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.172953 · Cited by 45
Corynebacterium tuberculostearicum, a human skin colonizer, induces the canonical nuclear factor‐κB inflammatory signaling pathway in human skin cells
Altonsy, M. O., Kurwa, H. A., Lauzon, G. J., Amrein, M., Gerber, A. N., Almishri, W., & Mydlarski, P. R. (2020) · Immunity Inflammation and Disease · doi:10.1002/iid3.284 · Cited by 42
“This enhances the transcription of target genes, including those encoding numerous inflammatory effector molecules.(41,42) Results presented above show the activation by infection with C.”
Background
MicroRNA-301b promotes cell proliferation and apoptosis resistance in triple-negative breast cancer by targeting CYLD
Song, H.-M., Li, D.-F., Wu, T.-Q., Xie, D., Hua, K., Hu, J., Deng, X.-C., Ji, C., Deng, Y.-J., & Fang, L. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.11.168 · Cited by 45
“The NF-B signaling pathway has key roles in inflammation, immune response, oncogenesis and protection against apoptosis (10, 11).”
Background
BST2 promotes cell proliferation, migration and induces NF-κB activation in gastric cancer
Liu, W., Cao, Y., Guan, Y., & Zheng, C.-Q. (2018) · Biotechnology Letters · doi:10.1007/s10529-018-2562-z · Cited by 45
PLCγ-dependent mTOR signalling controls IL-7-mediated early B cell development
Yu, M., Chen, Y., Zeng, H., Zheng, Y., Fu, G., Zhu, W., Broeckel, U., Aggarwal, P., Turner, A., Neale, G. A. M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01388-5 · Cited by 55
The NF-κB signaling network in the life of T cells
Daniëls, M. A., & Teixeiro, E. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1559494 · Cited by 50
The immunomodulatory effects of lactoferrin and its derived peptides on NF‐κB signaling pathway: A systematic review and meta‐analysis
Yami, H. A., Tahmoorespur, M., Javadmanesh, A., Tazarghi, A., & Sekhavati, M. (2023) · Immunity, Inflammation and Disease · doi:10.1002/iid3.972 · Cited by 44
“Pro‐inflammatory stimuli, such as LPS, and pro‐inflammatory cytokines, such as TNF‐α, IL‐6, and IL‐1β, cause phosphorylation and ubiquitination of IκB, which consequently leads to its proteasomal degradation.(16) IκB kinase (IKK) complex with three subunits, including IKKα, IKKβ, and IKK/NF‐κB essential modulator (NEM…”
Background
Natural Compounds for SIRT1‐Mediated Oxidative Stress and Neuroinflammation in Stroke: A Potential Therapeutic Target in the Future
Fang, C., Xu, H., Yuan, L., Zhu, Z., Wang, X., Liu, Y., Zhang, A., Shao, A., & Lou, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1949718 · Cited by 46
The immunoproteasome: An old player with a novel and emerging role in alloimmunity
Eskandari, S., Seelen, M., Lin, G., & Azzi, J. (2017) · American Journal of Transplantation · doi:10.1111/ajt.14435 · Cited by 44
Bupleurum chinense extract ameliorates an OVA-induced murine allergic asthma through the reduction of the Th2 and Th17 cytokines production by inactivation of NFκB pathway.
Bui, T. T., Chun, H.-P., Chang, H.-S., Shin, H., & Chai, O.-H. (2017) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2017.04.133 · Cited by 44
MicroRNA-377: A therapeutic and diagnostic tumor marker
Akhlaghipour, I., Taghehchian, N., Zangouei, A. S., Maharati, A., Mahmoudian, R. A., Saburi, E., & Moghbeli, M. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.11.236 · Cited by 40
A conserved long noncoding RNA, GAPLINC, modulates the immune response during endotoxic shock
Vollmers, A., Covarrubias, S., Kuang, D., Shulkin, A., Iwuagwu, J., Katzman, S., Song, R., Viswanathan, K., Vollmers, C., Wakeland, E., et al. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2016648118 · Cited by 43
“Upon activation, I-κ B-α is degraded, allowing p65:p50 to translocate into the nucleus and activate target genes (20).”
Analysis of chicken macrophage functions and gene expressions following infectious bronchitis virus M41 infection
Sun, X., Wang, Z., Shao, C., Yu, J., Liu, H., Chen, H., Li, L., Wang, X., Ren, Y., Huang, X., et al. (2021) · Veterinary Research · doi:10.1186/s13567-021-00896-z · Cited by 43
“Transcription factor Nuclear factor-κB (NF-κB) is a redox-sensitive transcription factor and modulates ILs production [46].”
Background
LIGHT aggravates sepsis‐associated acute kidney injury via TLR4‐MyD88‐NF‐κB pathway
Zhong, Y., Wu, S., Yang, Y., Li, G.-Q., Meng, L., Zheng, Q.-Y., Li, Y., Xu, G.-L., Zhang, K.-Q., & Peng, K.-F. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15815 · Cited by 43
Effects of Vaspin on Insulin Resistance in Rats and Underlying Mechanisms
Liu, S., Duan, R., Wu, Y., Du, F., Zhang, J., Li, X., Guo, S., Wang, M., Zhang, Q., Li, Y., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-31923-3 · Cited by 46
Benzo(a)pyrene in Cigarette Smoke Enhances HIV-1 Replication through NF-κB Activation via CYP-Mediated Oxidative Stress Pathway
Ranjit, S., Sinha, N., Kodidela, S., & Kumar, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-28500-z · Cited by 44
Effects of vaspin on pancreatic β cell secretion via PI3K/Akt and NF-κB signaling pathways
Liu, S., Li, X., Wu, Y., Duan, R., Zhang, J., Du, F., Zhang, Q., Li, Y., & Li, N. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189722 · Cited by 50
LIPUS suppressed LPS‐induced IL‐1α through the inhibition of NF‐κB nuclear translocation via AT1‐PLCβ pathway in MC3T3‐E1 cells
Nagao, M., Tanabe, N., Manaka, S., Naito, M., Sekino, J., Takayama, T., Kawato, T., Torigoe, G., Kato, S., Tsukune, N., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25777 · Cited by 43
“NF-κB p50 and p65 are existed as typical hererodimer (Karin & Ben-Neriah, 2000).”
Background
Anti-inflammatory Effects of Canthin-6-one Alkaloids from Ailanthus altissima
Cho, S.-K., Jeong, M., Jang, D., & Choi, J.-H. (2017) · Planta Medica · doi:10.1055/s-0043-123349 · Cited by 43
“It plays a critical role in inflammatory processes by regulating the expression of pro-inflammatory genes [23].”
Background
TMEM43/LUMA is a key signaling component mediating EGFR-induced NF-κB activation and tumor progression
Jiang, C.-Y., Zhu, Y., Zhou, Z.-C., Gumin, J., Bengtsson, L., Wu, W.-S., Zhou, S.-Y., Lang, F.-F., & Lin, X. (2017) · Oncogene · doi:10.1038/onc.2016.430 · Cited by 43
RSK2 and its binding partners in cell proliferation, transformation and cancer development
Cho, Y. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0880-z · Cited by 46
The nitrated fatty acid 10-nitro-oleate attenuates allergic airway disease
Reddy, A. T., Lakshmi, S. P., Dornadula, S., Pinni, S., Rampa, D. R., & Reddy, R. C. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300730 · Cited by 42
Monitoring the Levels of Cellular NF-κB Activation States
Meier‐Soelch, J., Mayr‐Buro, C., Juli, J. U., Leib, L., Linne, U., Dreute, J., Papantonis, A., Schmitz, M. L., & Kracht, M. (2021) · Cancers · doi:10.3390/cancers13215351 · Cited by 53
“Downstream of receptors, the various cytosolic activation pathways have in common that they involve the inducible formation of protein/protein interactions, which are controlled by highly regulated posttranslational modifications, primarily phosphorylation and ubiquitination [5,6].”
Background
CircNPHP4 in monocyte-derived small extracellular vesicles controls heterogeneous adhesion in coronary heart atherosclerotic disease
Xiong, F., Mao, R., Zhang, L., Zhao, R., Tan, K., Liu, C., Xu, J., Du, G., & Zhang, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04253-y · Cited by 51
Polysaccharide extracted from Potentilla anserina L ameliorate acute hypobaric hypoxia‐induced brain impairment in rats
Shi, J., Wang, J., Zhang, J., Li, X., Tian, X., Wang, W., Wang, P., & Li, M. (2020) · Phytotherapy Research · doi:10.1002/ptr.6691 · Cited by 42
Exploring Dysregulated Signaling Pathways in Cancer
Nisar, S., Hashem, S., Macha, M. A., Yadav, S. K., Muralitharan, S., Therachiyil, L., Sageena, G., Al‐Naemi, H. A., Haris, M., & Bhat, A. A. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200115095937 · Cited by 60
Saikosaponin B2 Suppresses Inflammatory Responses Through IKK/IκBα/NF-κB Signaling Inactivation in LPS-Induced RAW 264.7 Macrophages
Shin, J., Im, H., & Lee, K. (2018) · Inflammation · doi:10.1007/s10753-018-0898-0 · Cited by 47
Abietic acid attenuates RANKL induced osteoclastogenesis and inflammation associated osteolysis by inhibiting the NF‐KB and MAPK signaling
Thummuri, D., Guntuku, L., Challa, V. S., Ramavat, R. N., & Naidu, V. G. M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26575 · Cited by 45
“Upon cytokine stimulation, IKKmediates the proteosomal degradation of IκBα by phosphorylation of IκBα at ser32 and ser36 and liberates NF-κB leading to its nuclear translocation (Karin & Ben-Neriah, 2000; Siebenlist, Franzoso, & Brown, 1994).”
Background
NF-κB Members Left Home: NF-κB-Independent Roles in Cancer
Colomer, C., Marruecos, L., Vert, A., Bigas, A., & Espinosa, L. (2017) · Biomedicines · doi:10.3390/biomedicines5020026 · Cited by 52
ADAR1 deletion induces NFκB and interferon signaling dependent liver inflammation and fibrosis
Ben-Shoshan, S. O., Kagan, P., Sultan, M., Barabash, Z., Dor, C., Jacob-Hirsch, J., Harmelin, A., Pappo, O., Marcu-Malina, V., Ben-Ari, Z., et al. (2017) · RNA Biology · doi:10.1080/15476286.2016.1203501 · Cited by 42
“Importantly, the latter kinase is a major component of the IKK complex that initiates the signaling cascade resulting in IkB degradation and enhanced NFkB p65 transcriptional activity.(29,34) Moreover, we could partly prevent IL6 overproduction in ADAR1 KD cells, by expressing editase deficient p110 and p150 ADAR1 iso…”
Background
α-Cyperone of Cyperus rotundus is an effective candidate for reduction of inflammation by destabilization of microtubule fibers in brain
Azimi, A., Ghaffari, S. M., Riazi, G. H., Arab, S. S., Tavakol, M. M., & Pooyan, S. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.06.058 · Cited by 46
Advances in Understanding the Role of NRF2 in Liver Pathophysiology and Its Relationship with Hepatic-Specific Cyclooxygenase-2 Expression
Fuertes‐Agudo, M., Luque-Tévar, M., Cucarella, C., Martín‐Sanz, P., & Casado, M. (2023) · Antioxidants · doi:10.3390/antiox12081491 · Cited by 48
“The canonical pathway is triggered by Toll-like receptors (TLRs) and pro-inflammatory cytokines such as tumor necrosis factor alpha (TNFα) and interleukin (IL)-1, leading to the expression of nuclear factor NF-κB p65 subunit (RELA gene), which regulates the expression of pro-inflammatory and cell survival genes [58].”
PM2.5 exposure increases dry eye disease risks through corneal epithelial inflammation and mitochondrial dysfunctions
Yu, D., Cai, W., Shen, T., Wu, Y., Ren, C., Li, T., Hu, C., Zhu, M., & Yu, J. (2023) · Cell Biology and Toxicology · doi:10.1007/s10565-023-09791-z · Cited by 47
“The p65 subunit of NF-κB released from IκBα is subsequently phosphorylated by IKKβ or other kinases and moves into the nucleus (Karin and Ben-Neriah 2000).”
Background
Toxoplasma gondii Dense Granule Proteins 7, 14, and 15 Are Involved in Modification and Control of the Immune Response Mediated via NF-κB Pathway
Ihara, F., Fereig, R. M., Himori, Y., Kameyama, K., Umeda, K., Tanaka, S., Ikeda, R., Yamamoto, M., & Nishikawa, Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01709 · Cited by 47
“Upon exposure to various infectious and inflammatory stimuli, the inhibitor proteins are phosphorylated, resulting in their ubiquitination and degradation, allowing the nuclear translocation of NFκB dimers to regulate gene expression (10).”
Background
Long Non-Coding RNA-NEAT1 Promotes Cell Migration and Invasion via Regulating miR-124/NF-κB Pathway in Cervical Cancer
Shen, X.-F., Zhao, W., Zhang, Y., & Liang, B. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s220306 · Cited by 41
Annonaceae: Breaking the Wall of Inflammation
Attiq, A., Jalil, J., & Husain, K. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00752 · Cited by 48
“Upon receiving the stimulus, 26S proteosome seeks the help of IκB kinases for the phosphorylation and polyubiquition of IκB (Karin and Ben-Neriah, 2000; Broide et al., 2005).”
Background
Novel unsaturated glycyrrhetic acids derivatives: Design, synthesis and anti-inflammatory activity.
Li, B., Cai, S.-S., Yang, Y.-A., Chen, S.-C., Chen, R., Shi, J.-B., Liu, X.-H., & Tang, W.-J. (2017) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2017.08.002 · Cited by 40
“NFκB activation is controlled by phosphorylation and degradation of I κB-α, a cognate regulatory subunit of NFκB [40].”
Background
Protective effects of puerarin on acute lung and cerebrum injury induced by hypobaric hypoxia via the regulation of aquaporin (AQP) via NF-κB signaling pathway.
Wang, C., Yan, M.-Y., Jiang, H., Wang, Q., Guan, X., Chen, J., & Wang, C. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2016.09.010 · Cited by 40
Targeting STAT3 and NF-κB Signaling Pathways in Cancer Prevention and Treatment: The Role of Chalcones
Krajka‐Kuźniak, V., Belka, M., & Papierska, K. (2024) · Cancers · doi:10.3390/cancers16061092 · Cited by 43
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BackgroundInfluential
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Background

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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