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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Adiponectin alleviates blood hypercoagulability via inhibiting endothelial cell apoptosis induced by oxidative stress in septic rats.
Hou, Y., Wang, X., Lang, Z., Zhao, W., Jin, Y., Zhang, H., & Zhang, L. (2018) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2018.29389.7117 · Cited by 6
Josamycin suppresses Prevotella intermedia lipopolysaccharide-induced production of nitric oxide and interleukin-1β in murine macrophages.
Choi, E., Choe, S., Hyeon, J., Park, H., Choi, I., & Kim, S.-J. (2018) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2018.05.139 · Cited by 6
Prostate cancer tends to metastasize in the bone-mimicking microenvironment via activating NF-κB signaling
Tong, H.-B., Zou, C., Qin, S.-Y., Meng, J., Keller, E., Zhang, J., & Lu, Y. (2018) · Journal of Biomedical Research · doi:10.7555/jbr.32.20180035 · Cited by 6
Cardioprotective time‐window of Penehyclidine hydrochloride postconditioning: A rat study
Tan, H., Lin, D.-M., Wang, Z.-Q., Yang, Y.-L., & Ma, J. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.07.003 · Cited by 6
Structural Basis for the Activation of IKK1/α
Polley, S., Passos, D., Huang, D.-B., Mulero, M. C., Mazumder, A., Biswas, T., Verma, I. M., Lyumkis, D., & Ghosh, G. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.067 · Cited by 6
“, 1999) for the phosphorylation of specific residues of prototypical IκB proteins (IκBα, -β, and -ε) bound to NF-κB as well as an atypical IκB protein, NF-κB1/p105, which is the precursor of the NF-κB subunit p50 (Karin and Ben-Neriah, 2000).”
Dietary Polyphenols as Natural Modulators of NF‐κB Signaling in Inflammation‐Driven Non‐Communicable Diseases: Focus on Cancer
Dinislam, K., Shamsi, A., Tasqeruddin, S., & Shahwan, M. (2026) · Food Science & Nutrition · doi:10.1002/fsn3.72027 · Cited by 5
A novel phosphodiesterase 5 inhibitor, CPD1, alleviates liver fibrosis by modulating the Akt/NF-κB pathway to inhibit activated hepatic stellate cells
Feng, W., Feng, W., 杨俭勤, Li, L., Li, L., Shan, C., Chen, S., Zhao, Z., 赵正刚, Zhou, S., et al. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117388 · Cited by 6
Lycium barbarum Polysaccharides Suppress Radiation-Induced Microglial Inflammation by Inhibiting the IKKβ/IκBα/NF-κB Pathway
Zhang, X., Liu, Q., Liu, L., Qian, F., Ren, B.-X., & Tang, F.-R. (2025) · Dose-Response · doi:10.1177/15593258251382964 · Cited by 5
How transcription factors regulate apoptosis in endometriosis (Review)
Ouyang, Z., Deng, J., Zhang, L., & Shen, F. (2025) · Molecular Medicine Reports · doi:10.3892/mmr.2025.13654 · Cited by 6
Crebanine protects against ovariectomy-induced bone loss by targeting Sirt1 to interfere with NF-κB acetylation and ROS activity
Zhang, H., Zhao, X., Wang, Z., Miao, J., Hu, X., Cui, P., Jin, C., Zhao, X., Liang, H., Ye, H., et al. (2025) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2025.101426 · Cited by 5
RNA polymerase II subunit 5-mediating protein limits TLR4-induced innate immune activation in macrophages by inhibiting IKKβ/NF-κB signaling during sepsis
Pang, S.-J., Jiang, T.-Y., Wang, N., Cui, X., Wang, H., Pan, Y.-F., Yang, N., & Dong, L.-W. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02278-w · Cited by 5
Zebrafish TDP43 positively regulates p65-mediated apoptotic pathway.
Yu, T.-T., Li, M.-M., Li, M.-F., Zhang, Q.-L., Zhang, H., Jiang, Z.-Y., Wang, S.-H., Mao, H.-L., Li, D.-M., Fan, L.-H., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142599 · Cited by 5
The role of glutathione S-transferase mu 2 in mitigating fatty acid-induced hepatic inflammation in dairy cows.
Li, J., Zhao, C.-C., Qi, D., Kong, F.-R., Liu, M., Gao, J., Li, E., Gao, W., Du, X., Song, Y.-X., et al. (2025) · Journal of Dairy Science · doi:10.3168/jds.2024-25740 · Cited by 5
Melatonin and retinal cell damage: molecular and biological functions
Sun, J., Liu, Y., & Chen, Z.-M. (2024) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-024-03575-w · Cited by 5
“…the alternative pathway comprises the activation of NF-κB by a variety of molecules including lympho-toxin β (TNFSF3), CD40 ligand, B cell activating factor, and receptor activator of NF-κB ligand (RANKL) (Karin and Ben-Neriah 2000; Senftleben et al. 2001; Bonizzi et al. 2004; Novack et al. 2003).”
ApoA-I binding protein (AIBP) regulates transient receptor potential vanilloid 1 (TRPV1) activity in rat dorsal root ganglion neurons by selective disruption of toll-like receptor 4 (TLR4)-lipid rafts
Li, Y., Uhelski, M. L., North, R. Y., Farson, L. B., Bankston, C. B., Roland, G. H., Fan, D. H., Sheffield, K. N., Jia, A., Orlando, D., et al. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.10.017 · Cited by 5
Insights into the mechanism of transcription factors in Pb2+-induced apoptosis
Guo, J., Li, R., Ouyang, Z., Tang, J., Zhang, W., Chen, H., Zhu, Q., Zhang, J., & Zhu, G. (2024) · Toxicology · doi:10.1016/j.tox.2024.153760 · Cited by 5
Malva parviflora seed oil; Isolation, gas chromatographic profiling and its cardioprotective activity against myocardial infraction in animal model
Hussein, M. A., Islam, M. S., Ali, A. A., Mansour, M. S., Bondok, M. S., Salem, M. A., Amein, A., & El-gizawy, H. A. (2023) · Journal of King Saud University: Science · doi:10.1016/j.jksus.2023.103060 · Cited by 5
Molecular characterization and functional analysis of a mollusk Rel homologous gene.
Chen, J., Ma, J., Cui, J., Zhang, G., Dong, J., Yu, T., Zheng, Y.-X., Qu, Y., Cai, S., Lu, X.-Q., et al. (2023) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2023.109188 · Cited by 5
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
Borar, P., Biswas, T., Chaudhuri, A., Rao, P. T., Raychaudhuri, S., Huxford, T., Chakrabarti, S., Ghosh, G., & Polley, S. (2023) · bioRxiv · doi:10.1101/2023.06.27.546692 · Cited by 5
Animal venoms: a novel source of anti-Toxoplasma gondii drug candidates
Yang, D., Liu, X., Li, J., Xie, J., & Jiang, L.-P. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1178070 · Cited by 5
Fentanyl inhibits cell invasion and migration by modulating NF-κB activation in glioma.
Liu, D., & Xu, S.-Y. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148356 · Cited by 5
Alteration in branching morphogenesis via YAP/TAZ in fibroblasts of fetal lungs in an LPS-induced inflammation model
Ko, H.-S., Laiman, V., Tsao, P.-N., Chen, C.-M., & Chuang, H.-C. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00613-w · Cited by 5
“Phosphorylation of IκB activates nuclear factor (NF)-κB, which is regarded as a proinflammatory signal pathway (Karin and Ben-Neriah 2000; Lawrence 2009).”
Background
Modulation of Kinase Activities In Vitro by Hepatitis C Virus Protease NS3/NS4A Mediated-Cleavage of Key Immune Modulator Kinases
Abdullah, M. A. F., McWhirter, S. M., & Suo, Z. (2023) · Cells · doi:10.3390/cells12030406 · Cited by 5
“IKKβ is primarily responsible for the phosphorylation of specific residues of prototypical IκB proteins (IκBα, IκBβ, and IκBε) bound to NF-κB as well as an atypical IκB protein, p105, which is the precursor of the NF-κB subunit p50 [36].”
Background
Tyrosine phosphatase STEP is a key regulator of glutamate-induced prostaglandin E2 release from neurons
Rajagopal, S., Poddar, R., & Paul, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100944 · Cited by 5
“To clarify the role of NF-κB in glutamate-NMDAR–induced activation of the COX2/PGE2 signaling pathway in STEP KO mice neurons, we next evaluated the effect of glutamate on inhibitor of nuclear factorκB (IκB) degradation, a seminal step in NF-κB activation (34, 35).”
Method
Single loss of a Trp53 allele triggers an increased oxidative, DNA damage and cytokine inflammatory responses through deregulation of IκBα expression
Marruecos, L., Manils, J., Moreta-Moraleda, C., Gómez, D., Filgaira, I., Serafín, A., Cañas, X., Espinosa, L., & Soler, C. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03638-3 · Cited by 6
Gosha-jinki-Gan (GJG) shows anti-aging effects through suppression of TNF-α production by Chikusetsusaponin V.
Hagihara, K., Nunomura, K., Lin, B., Fumimoto, M., Watanabe, J., & Mizuhara, Y. (2021) · Gene · doi:10.21203/rs.3.rs-189204/v1 · Cited by 5
Adoptive transfer of immature myeloid cells lacking NF‐κB p50 (p50‐IMC) impedes the growth of MHC‐matched high‐risk neuroblastoma
Cui, C., Barberi, T., Suresh, R., & Friedman, A. (2021) · Molecular Oncology · doi:10.1002/1878-0261.12904 · Cited by 5
Nuclear Factor-κB Activating Protein Plays an Oncogenic Role in Neuroblastoma Tumorigenesis and Recurrence Through the Phosphatidylinositol 3-Kinase/Protein Kinase B Signaling Pathway
Liu, J., Zhang, M.-Y., Kan, Y., Wang, W., Liu, J., Gong, J.-H., & Yang, J.-G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.622793 · Cited by 5
“Nuclear factor-κB (NF-κB) is a transcription factor found in essentially all cell types and regulates the transcription of numerous genes involved in infection, inflammation, immunity, and cancer (Karin and Ben-Neriah, 2000).”
Background
Tricarbonyldichlororuthenium(II) dimer, the lipid-soluble carbon monoxide-releasing molecule, attenuates Prevotella intermedia lipopolysaccharide-induced production of nitric oxide and interleukin-1β in murine macrophages.
Choi, E., Keum, B., Choe, S., Hyeon, J., Choi, I., & Kim, S.-J. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107190 · Cited by 5
Development and characterization of a novel, megakaryocyte NF‐κB reporter cell line for investigating inflammatory responses
Vallance, T. M., Sheard, J., Meng, Y., Torre, E. C., Patel, K., Widera, D., & Vaiyapuri, S. (2020) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.15118 · Cited by 5
Diabetic retinopathy its genetics and single nucleotide polymorphism associated with multi-ethnic cohort – A review
Thiruchelvi, R., & Raghunathan, K. (2020) · Materials Today Proceedings · doi:10.1016/j.matpr.2020.07.178 · Cited by 5
Molecular cloning, functional characterization and expression analysis of P65 subunit in response to GCRV infection in rare minnow (Gobiocypris rarus).
Zhou, M., Wang, B., Lin, Y., Zhang, C., & Cao, H. (2020) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2020.103786 · Cited by 5
Design and development of novel thiazolidin‐4‐one‐1,3,5‐triazine derivatives as neuro‐protective agent against cerebral ischemia–reperfusion injury in mice via attenuation of NF‐ĸB
Lu, M., Qi, Y., Han, Y.-C., Yi, Q., Xu*, L., Sun, W.-L., Ni, G., Ni, X., & Xu, C.-S. (2020) · Chemical Biology and Drug Design · doi:10.1111/cbdd.13744 · Cited by 5
A Novel Screening Approach for the Dissection of Cellular Regulatory Networks of NF-κB Using Arrayed CRISPR gRNA Libraries
O'Shea, P. J., Wildenhain, J., Leveridge, M., Revankar, C. M., Yang, J., Bradley, J., Firth, M. A., Pilling, J. E., Piper, D. R., Chesnut, J. D., et al. (2020) · SLAS DISCOVERY · doi:10.1177/2472555220926160 · Cited by 7
A reaction-diffusion network model predicts a dual role of Cactus/IκB to regulate Dorsal/NFκB nuclear translocation in Drosophila
Barros, C. D. T., Cardoso, M., Bisch, P., Araujo, H., & Lopes, F. P. (2020) · bioRxiv · doi:10.1371/journal.pcbi.1009040 · Cited by 5
Evaluation of Physiological Functionalities and Anti-inflammatory Activity on in vitro Cultured Adventitious Root of Platycodon grandiflorum
Boo, H., Park, J.-H., Kim, H.-H., Kwon, S.-J., & Woo, S. (2018) · Journal of Crop Science and Biotechnology · doi:10.1007/s12892-018-0101-0 · Cited by 5
The E3 ubiquitin ligase MuRF2 attenuates LPS‐induced macrophage activation by inhibiting production of inflammatory cytokines and migration
Bian, H.-J., Gao, S.-S., Zhang, D., Zhao, Q., Li, F.-F., Li, X., Sun, S., Song, S., Li, T., Zhu, Q., et al. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12367 · Cited by 5
The effects of interleukin-1 beta and gamma-quantum braking radiation on mesenchymal progenitor cells
Bigildeev, A., Zezina, E. A., & Drize, N. (2017) · Molecular Biology · doi:10.1134/s0026893317020054 · Cited by 5
“Phosphorylated IkB proteins are subjected to polyubiquitination and subsequent degradation or fragmentation in proteasomes [11].”
Nuclear Receptor PPARα Agonist Wy-14,643 Ameliorates Hepatic Cell Death in Hepatic IKKβ-Deficient Mice
Kim, T., Wahyudi, L. D., Gonzalez, F., & Kim, J.-H. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2016.218 · Cited by 5
Targeting NF-κB-inducing kinase (NIK) in the non-canonical pathway: Advances in the development of NIK inhibitors.
Huang, X., Li, R., Zong, M., Zhu, Y., Sun, Y., & Cui, H. (2025) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2025.109247 · Cited by 4
HTATSF1 regulates innate antiviral immune response by orchestrating TRAF3-IRF3 and TRAF6-NF-κB pathways
Zeng, J., Ruan, Z., Zhang, Q., Yi, X.-M., Chen, Y.-D., Hu, M.-M., & Li, S. (2025) · Cell Insight · doi:10.1016/j.cellin.2025.100294 · Cited by 4
Pulchinenoside C Attenuates the Development of Osteoarthritis by Inhibiting the PI3K/AKT/NF‐κB Signalling Pathway
Hu, J., Xiao, K., Liang, J., Yu, X., Zhu, M., Kuang, Z.-H., Shi, S.-J., Zhang, B., & Xu, Q. (2025) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70738 · Cited by 4
“The free NF-κB complex is transported to the nucleus, which activates the expression of proinflammatory and destructive mediators (e.g., cyclooxygenase 2 [COX2] and prostaglandin E2 [PGE2], inducible nitric oxide synthase [iNOS] and catabolic enzymes [ADAMTS5 and MMP13]) [48–50].”
Deficiency of Cartilage‐Specific Y‐Box Binding Protein 1 Represses NF‐κB Signaling and Alleviates Osteoarthritis Progression
Li, X., Zhang, Z., Xie, J., Guo, W., Deng, Z., & Huang, Z.-Y. (2025) · Arthritis & Rheumatology · doi:10.1002/art.43311 · Cited by 4
“41,42 For example, when DNA damage occurs, the N-terminal region of p53 is phosphorylated, which reduces the binding between p53 and murine double minute 2, decreasing the ubiquitination of p53.”
The E3 ubiquitin ligase STUB1 inhibits glioblastoma progression though promoting IKKα ubiquitination and blocking NF-κB signaling pathway
Zhang, D., Chen, S., Peng, W., Liu, G., Zhang, Q., Ghani, M. U., Zhou, P., Zhao, H., Liang, P., & Cui, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.146064 · Cited by 5
Investigating Natural Product Inhibitors of IKKα: Insights from Integrative In Silico and Experimental Validation
Yasir, M., Park, J., Han, E.-T., Han, J.-H., Park, W., Choe, J., & Chun, W. (2025) · Molecules · doi:10.3390/molecules30092025 · Cited by 4
Regulation of PEST-containing nuclear proteins in cancer cells: implications for cancer biology and therapy
Jiang, K., Zhu, Y.-H., Jiang, Z., Liu, Y., Hussain, W., Luo, H.-Y., Sun, W.-H., Ji, X.-Y., & Li, D. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1548886 · Cited by 4
“In several signaling pathways, ubiquitination controls the location and activity of crucial protein kinases and the amounts of protein substrate (68).”
Contagious ecthyma in small ruminants: from etiology to vaccine challenges - a review
Reichen, C., Beirão, B. C. B., & Monteiro, A. L. G. (2025) · Veterinary Research Communications · doi:10.1007/s11259-025-10677-0 · Cited by 8
“This degradation allows NF-κB subunits to translocate to the nucleus, where they modulate the expression of target genes (Karin and Ben-Neriah 2000).”
TRIM21 interacts with IκBα and negatively regulates NF-κB activation in Corynebacterium pseudotuberculosis-infected macrophages.
Wu, C., Wang, X., Li, X., Li, H.-X., Peng, Q., Niu, X., Wu, Y., Wang, Z.-Y., & Zhou, Z.-Y. (2025) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2025.110910 · Cited by 4
GILT stabilizes cofilin to promote the metastasis of prostate cancer
Han, D.-S., Wu, Z., Zhang, C., Wei, Z.-W., Chao, F., Xie, X.-F., Liu, J.-K., Song, Y.-F., Song, X.-M., Shao, D.-C., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02288-0 · Cited by 4
F-box protein Fbx23 acts as a transcriptional coactivator to recognize and activate transcription factor Ace1
Liu, Z., Ma, K., Zhang, P., Zhang, S., Song, X., & Qin, Y.-Q. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011539 · Cited by 4
“For instance, mammal nuclear factor-kappaB activation represents a paradigm for controlling the function of a transcription factor via proteolysis; NF-kappaB precursors are processed into mature active forms of smaller proteins by the UPS [62].”
Tremella fuciformis Berk Alleviated Atherosclerosis Symptoms via Nuclear Factor-Kappa B-Mediated Inflammatory Response in ApoE−/− Mice
Dong, Y., Zhang, Q. X., Xie, R., Zhao, J., Han, Z., Li, Y., Yu, H., & Zhang, Y. (2024) · Nutrients · doi:10.3390/nu17010160 · Cited by 13
“Consequently, IKK α + β governs the expression of a multitude of inflammation-related genes within cells and modulates inflammatory responses by regulating the NF-κ B signaling pathway [65].”
Cystathionine γ-lyase contributes to exacerbation of periodontal destruction in experimental periodontitis under hyperglycemia.
Song, D., He, J.-F., Cheng, T.-F., Jin, L.-J., Li, S.-J., Chen, B., Li, Y.-M., & Liao, C.-S. (2024) · The Journal of Periodontology · doi:10.1002/jper.23-0811 · Cited by 4
Cichorium intybus L. significantly alleviates cigarette smoke-induced acute lung injury by lowering NF-κB pathway activation and inflammatory mediators
Hussain, N., Ikram, N., Khan, K. U. R., Hussain, L., Alqahtani, A. M., Alqahtani, T., Hussain, M., Suliman, M., Alshahrani, M., & Sitohy, B. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22055 · Cited by 4
“Due to the action of the inhibitory protein I κ B, in particular I κ B α , NF-κ B remains dormant in the cytoplasm of unstimulated cells [22,23].”
Background
Tmem178 negatively regulates IL-1β production through inhibition of the NLRP3 inflammasome
Khanna, K., Yan, H., Mehra, M., Rohatgi, N., Mbalaviele, G., & Faccio, R. (2023) · bioRxiv · doi:10.1101/2023.03.07.531385 · Cited by 4
“Similar to osteoclasts (15), we did not detect differences in the phosphorylation and degradation of IκB-α, a readout for NF-κB activation (20), between WT and Tmem178-/- bone marrow derived macrophages (BMDMs) stimulated with LPS (Supplemental Fig.”
Background
Nitrooleic acid inhibits macrophage activation induced by lipopolysaccharide from Prevotella intermedia
Choi, E., Lee, J. E., Lee, A. R., Choi, I. S., & Kim, S. (2022) · Nutrition Research · doi:10.1016/j.nutres.2022.07.009 · Cited by 5
Integrative Proteomic Analysis of Posttranslational Modification in The Inflammatory Response
Ji, F., Zhou, M.-H., Zhu, H.-H., Jiang, Z.-Y., Li, Q.-R., Ouyang, X., Lv, Y.-M., Zhang, S., Wu, T., & Li, L.-J. (2020) · bioRxiv · doi:10.1101/2020.07.20.212134 · Cited by 4
Protective effects of andrographolide on lead-induced kidney injury through inhibiting inflammatory and oxidative responses in common carp
Zhang, Y., Zhang, P.-J., Yu, P., Shang, X., Fu, Y., Lu, Y.-T., & Li, Y.-H. (2020) · doi:10.1016/j.aqrep.2020.100395 · Cited by 4
Primaquine phosphate induces the apoptosis of ATRA‐resistant acute promyelocytic leukemia cells by inhibition of the NF‐κB pathway
Ma, L., Chen, L., Li, H., Ge, L., Wang, S.-H., Zhang, Z.-D., Huang, H., Shi, L.-Z., Li, T., Gu, H.-H., et al. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3a0120-061rr · Cited by 4
Yiqi-Huoxue Granule (YQHX) Downregulates Prothrombotic Factors by Modulating KLF2 and NF-κB in HUVECs following LPS Stimulation
Wu, H., Wang, X., Gao, S.-B., Dai, L.-P., Tong, H., Gao, H., Lei, Z., Han, Y., Wang, Z.-T., Han, L.-H., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9425183 · Cited by 4
“Various inflammatory stimuli activate the NF-κB pathway by inducing the phosphorylation and degradation of IκBs [41, 42].”
Background
Retracted
Targeting cytokines in the 5-Lox pro-inflammatory pathway for treatment-resistant anorexia nervosa
Brooks, S. (2018) · Journal of Molecular and Genetic Medicine · doi:10.4172/1747-0862.1000376 · Cited by 4
“ILs trigger – in a feedback loop – the ‘canonical’ inflammatory pathway leading to activation of protein complexes, which cause NF-κβ to translocate across the nuclear membrane, genetically upregulating the inflammatory response [8].”
Background
Anti-neuroinflammatory effects of tryptanthrin from Polygonum tinctorium Lour. in lipopolysaccharide-stimulated BV2 microglial cells
Lee, S., Kim, D.-C., Baek, H., Lee, K., Kim, Y.-C., & Oh, H. (2018) · Archives of pharmacal research · doi:10.1007/s12272-018-1020-8 · Cited by 3
“Once cells are activated by inflammatory stimuli such as TNF-a and LPS, IjB-a is degraded and phosphorylated following in freeing active form p65/p50 (Lappas et al. 2002; Karin and Ben-Neriah 2000).”
BackgroundInfluential
Crosstalk of thioredoxin system and programmed cell death: from pathophysiology to novel therapy
Wu, Y., Su, Y., Pan, F., Jin, F., Huang, H., Deng, A., Lu, Y., Lu, Y., Li, T., Du, J., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104209 · Cited by 4
“A pro-oxidant state and cysteine oxidation promote NF-κ B nuclear translocation, allowing for target gene regulations [101,103 – 105].”
The Role of NF-κB in Peritoneal Fibrosis and Adhesion in Humans and Animals: A Systematic Review
Jasiński, T., Kozłowska, N., Zdrojkowski, L., Bręborowicz, A., Rey, B., & Domino, M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052199 · Cited by 3
The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling
Huang, W.-R., Li, J.-Y., Liao, T.-L., Lye, L.-F., Munir, M., & Liu, H.-J. (2025) · Journal of Virology · doi:10.1128/jvi.01089-25 · Cited by 3
Total Extract of Folium Rhododendri Daurici alleviate MASLD by regulating PPAR and TNF signaling pathways
Zhang, Y., Yin, Z., Zhang, Y., Wei, Y., Zhai, Y., Zhao, X., Zhan, B., Wang, Z., & Feng, H. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120955 · Cited by 4
Natural products as therapeutic interventions for inflammation-mediated cancer
Roy, S., Shaw, R., Pandey, A., & Trigun, S. K. (2025) · Discover Oncology · doi:10.1007/s12672-025-03004-1 · Cited by 4
Deciphering the Role of Macrophages in RSV Infection and Disease
Looy, S. V., Fransen, A., Jacobs, L., Schaerlaekens, S., Ceconi, M., Serrano‐Cano, F. I., Hudda, N. U., Moll, L. V., Smedt, M. D., Cos, P., et al. (2025) · Viruses · doi:10.3390/v17101351 · Cited by 3
Activation of NF‐κB Signaling by Optogenetic Clustering of IKKα and β
Fischer, A., Kramer, M. M., Baños, M., Grimm, M. M., Fliegauf, M., Grimbacher, B., Radziwill, G., Rahmann, S., & Weber, W. (2025) · Advanced Biology · doi:10.1002/adbi.202400384 · Cited by 4
A new mechanism of high-altitude adaptation reducing myocardium infarction: inhibiting inflammation-induced ubiquitin degradation of BKCa to enhance coronary vasodilation
Wang, S., Zhang, Y., Yuan, W.-C., Qi, C.-Y., Zhang, H.-X., Wang, T., Liu, H., Li, H.-S., Tian, Y., Wang, S., et al. (2025) · Basic Research in Cardiology · doi:10.1007/s00395-025-01113-0 · Cited by 4
High-Resolution Tracking of Aging-Related Small Molecules: Bridging Pollutant Exposure, Brain Aging Mechanisms, and Detection Innovations
Yu, K., Yang, S., Song, H., Sun, Z., Wang, K., Zhu, Y., Yang, C., Hao, R., & Cao, Y. (2025) · Biosensors · doi:10.3390/bios15040242 · Cited by 2
“…pathway, leading to the degradation of I κ B, the release of NF-κ B and its translocation into the nucleus, which in turn initiates the transcription of inflammation-related genes, resulting in a significant increase in the expression of pro-inflammatory cytokines such as TNF-α and IL-6 [37,39].”
Influential
Proteasome Inhibitors: Potential in Rheumatoid Arthritis Therapy?
Tarjányi, O., Olasz, K., Rátky, F., Sétáló, G., & Boldizsár, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26072943 · Cited by 3
Mitoxantrone attenuates lipopolysaccharide-induced acute lung injury via inhibition of NEDD8 activating enzyme.
Liu, H., Liu, Y., Lin, X., Fan, J.-H., Huang, Z., & Li, A. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113605 · Cited by 3
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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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