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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E3 ubiquitin ligase gene BIRC3 modulates TNF-induced cell death pathways and promotes aberrant proliferation in rheumatoid arthritis fibroblast-like synoviocytes
Meng, Q., Wei, K., & Shan, Y. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1433898 · Cited by 44
Structural and Functional Basis of JAMM Deubiquitinating Enzymes in Disease
Pan, X., Wu, S., Wei, W., Chen, Z., Wu, Y., & Gong, K. (2022) · Biomolecules · doi:10.3390/biom12070910 · Cited by 41
Pseudorabies Virus Infection of Epithelial Cells Leads to Persistent but Aberrant Activation of the NF-κB Pathway, Inhibiting Hallmark NF-κB-Induced Proinflammatory Gene Expression
Romero, N., Waesberghe, C. V., & Favoreel, H. W. (2020) · Journal of Virology · doi:10.1128/jvi.00196-20 · Cited by 34
Neuroprotective and Anti-inflammatory Effects of Pterostilbene Metabolites in Human Neuroblastoma SH-SY5Y and RAW 264.7 Macrophage Cells
Peñalver, P., Zodio, S., Lucas, R., de‐Paz, M. ‐., & Morales, J. C. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b07147 · Cited by 38
Rhizopus nigricans polysaccharide activated macrophages and suppressed tumor growth in CT26 tumor-bearing mice.
Wei, Z., Chen, G.-C., Zhang, P.-Y., Zhu, L., Zhang, L.-N., & Chen, K.-S. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.06.076 · Cited by 35
Ameliorative effects and possible molecular mechanisms of action of fibrauretine from Fibraurea recisa Pierre on d-galactose/AlCl3-mediated Alzheimer's disease
Xing, Z.-H., He, Z.-M., Wang, S., Yan, Y., Zhu, H.-Y., Gao, Y.-G., Zhao, Y., & Zhang, L.-X. (2018) · RSC Advances · doi:10.1039/c8ra05356a · Cited by 35
Dual Roles for Ikaros in Regulation of Macrophage Chromatin State and Inflammatory Gene Expression
Oh, K., Gottschalk, R. A., Lounsbury, N., Sun, J., Dorrington, M. G., Baek, S., Sun, G., Wang, Z., Krauss, K. S., Milner, J. D., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800158 · Cited by 39
Oxidized LDL-induced JAB1 influences NF-κB independent inflammatory signaling in human macrophages during foam cell formation
Schwarz, A., Bonaterra, G., Schwarzbach, H., & Kinscherf, R. (2017) · Journal of Biomedical Sciences · doi:10.1186/s12929-017-0320-5 · Cited by 35
“(PDF 264 kb) Additional file 5: OxLDL-induced NF-κB signaling in human MФ after 24 h. (PDF 340 kb) Abbreviations ABCA1: ATP-binding cassette protein A1; ANOVA: Analysis of variance; apoA1: Apolipoprotein A-1; apoE: Apolipoprotein E; BCA: Bicinchoninic acid; CCL2: C-C motif chemokine ligand 2; CE: Cholesteryl ester; CE…”
Background
Histone deacetylase 4 inhibits NF-κB activation by facilitating IκBα sumoylation
Yang, Q., Tang, J., Xu, C., Zhao, H., Zhou, Y., Wang, Y., Yang, M., Chen, X., & Chen, J. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaa043 · Cited by 35
Immuno-modulatory effect of probiotic E. coli Nissle 1917 in polarized human colonic cells against Campylobacter jejuni infection
Helmy, Y. A., Kassem, I. I., & Rajashekara, G. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1857514 · Cited by 42
MYD88 L265P elicits mutation-specific ubiquitination to drive NF-κB activation and lymphomagenesis
Yu, X., Li, W., Deng, Q., Liu, H., Wang, X., Hu, H., Cao, Y., Xu-Monette, Z. Y., Li, L., Zhang, M., et al. (2020) · Blood · doi:10.1182/blood.2020004918 · Cited by 43
Probiotic mediated NF-κB regulation for prospective management of type 2 diabetes
Bhardwaj, R., Singh, B. P., Sandhu, N., Singh, N., Kaur, R., Rokana, N., Singh, K. S., Chaudhary, V., & Panwar, H. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05254-4 · Cited by 38
Agomelatine prevents indomethacin-induced gastric ulcer in rats
Eraslan, E., Tanyeli̇, A., Güler, M. C., Kurt, N., & Yetim, Z. (2020) · Pharmacological Reports · doi:10.1007/s43440-019-00049-2 · Cited by 32
Ubiquitination in melanoma pathogenesis and treatment
Ma, J., Guo, W., & Li, C. (2017) · Cancer Medicine · doi:10.1002/cam4.1069 · Cited by 35
(DEAD)-box RNA helicase 3 modulates NF-κB signal pathway by controlling the phosphorylation of PP2A-C subunit
Wang, X., Wang, R., Luo, M., Li, C., Wang, H.-X., Huan, C., Qu, Y., Liao, Y., & Mao, X. (2017) · Oncotarget · doi:10.18632/oncotarget.16593 · Cited by 33
“NF-κB mainly distributes in the cytoplasm by interacting with the inhibitory IκB proteins (IκBα, IκBβ, IκBɛ and Bcl-3) [43].”
Serum- and Glucocorticoid-Inducible Kinase 1 Sensitive NF-κB Signaling in Dendritic Cells
Schmid, E., Xuan, N. T., Zahir, N., Russo, A., Yang, W., Kuhl, D., Faggio, C., Shumilina, E., & Lang, F. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000366311 · Cited by 33
Polygonatum sibiricum polysaccharides protect against knee osteoarthritis by inhibiting the TLR2/NF-κB signaling pathway in vivo and in vitro.
Kuang, S.-D., Liu, Z.-W., Liu, L., Fu, X., Sheng, W., Hu, Z., Lin, C., He, Q.-H., Chen, J., & Gao, S.-G. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133137 · Cited by 33
IFI44 is an immune evasion biomarker for SARS-CoV-2 and Staphylococcus aureus infection in patients with RA
Zheng, Q., Wang, D., Lin, R., Lv, Q., & Wang, W. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1013322 · Cited by 38
Anoikis resistance in diffuse glioma: The potential therapeutic targets in the future
Zhu, Z., Fang, C., Xu, H., Yuan, L., Du, Y., Ni, Y., Xu, Y., Shao, A., Zhang, A., & Lou, M. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.976557 · Cited by 37
p53/NF-kB Balance in SARS-CoV-2 Infection: From OMICs, Genomics and Pharmacogenomics Insights to Tailored Therapeutic Perspectives (COVIDomics)
Milani, D., Caruso, L., Zauli, E., Owaifeer, A. M. A., Secchiero, P., Zauli, G., Gemmati, D., & Tisato, V. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.871583 · Cited by 37
D-Limonene Is a Potential Monoterpene to Inhibit PI3K/Akt/IKK-α/NF-κB p65 Signaling Pathway in Coronavirus Disease 2019 Pulmonary Fibrosis
Yang, F., Chen, R., Li, W.-Y., Zhu, H.-Y., Chen, X.-X., Hou, Z.-F., Cao, R.-S., Zang, G., Li, Y., & Zhang, W. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.591830 · Cited by 26
Plant Polyphenols-Biofortified Foods as a Novel Tool for the Prevention of Human Gut Diseases
Scarano, A., Chieppa, M., & Santino, A. (2020) · Antioxidants · doi:10.3390/antiox9121225 · Cited by 40
“Other signaling pathways modulated by polyphenols participate to the inflammatory responses, proliferation and apoptosis, as in the case of the NFkB signaling pathway (Nuclear Factor kappa-light-chain enhancer of activated B cells [59]), and the MAP kinases pathway (Mitogen-Activated Protein kinase; [3,60]).”
Background
Characterization of the black carp TRAF6 signaling molecule in innate immune defense
Jiang, S., Xiao, J., Li, J., Chen, H., Wang, C., Feng, C., & Feng, H. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.06.011 · Cited by 35
18α-Glycyrrhetinic acid monoglucuronide as an anti-inflammatory agent through suppression of the NF-κB and MAPK signaling pathway.
Li, B., Yang, Y.-A., Chen, L., Chen, S.-C., Zhang, J., & Tang, W.-J. (2017) · MedChemComm · doi:10.1039/c7md00210f · Cited by 33
Resolving neuroinflammation, the therapeutic potential of the anti-malaria drug family of artemisinin
Shi, Z., Chen, Y., Lu, C., Dong, L.-M., Lv, J.-W., Tuo, Q.-H., Qin, L., Cheng, S.-W., Bu, L.-L., Lin, N., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.002 · Cited by 32
Critical Signaling Transduction Pathways and Intestinal Barrier: Implications for Pathophysiology and Therapeutics
Gao, J., Cao, B., Zhao, R., Li, H., Xu, Q., & Wei, B. (2023) · Pharmaceuticals · doi:10.3390/ph16091216 · Cited by 40
Vibrio harveyi infections induce production of proinflammatory cytokines in murine peritoneal macrophages via activation of p38 MAPK and NF-κB pathways, but reversed by PI3K/AKT pathways.
Yu, G.-R., Yu, H.-S., Yang, Q., Wang, J.-X., Fan, H., Liu, G., Wang, L., Bello, B., Zhao, P.-P., Zhang, H.-G., et al. (2021) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2021.104292 · Cited by 32
Recent trends of NFκB decoy oligodeoxynucleotide-based nanotherapeutics in lung diseases.
Mehta, M., Paudel, K., Shukla, S., Allam, V., Kannaujiya, V., Panth, N., Das, A., Parihar, V., Chakraborty, A., Ali, M., et al. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.08.010 · Cited by 32
“IκKB subunit of the IKK complex which in turn results in the ubiquitination and phosphorylation of two N-terminal serine residues of IκBα proteins [36].”
Background
β-hydroxybutyrate (β-HB) exerts anti-inflammatory and antioxidant effects in lipopolysaccharide (LPS)-stimulated macrophages in Liza haematocheila
Qiao, G., Lv, T., Zhang, M., Chen, P., Sun, Q., Zhang, J., & Li, Q. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.11.005 · Cited by 33
The effects of malvidin on oxidative stress parameters and inflammatory cytokines in LPS‐induced human THP‐1 cells
Bastin, A., Sadeghi, A., Nematollahi, M., Abolhassani, M., Mohammadi, A., & Akbari, H. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30049 · Cited by 32
Mannan-Binding Lectin Suppresses Peptidoglycan-Induced TLR2 Activation and Inflammatory Responses
Wang, F., Lǐ, Y., Yang, C., Mu, Y., Wang, Y., Zhang, W., Yang, Y., Chen, C., Song, S., Shen, Z., et al. (2019) · Mediators of Inflammation · doi:10.1155/2019/1349784 · Cited by 30
Mollugin Has an Anti-Cancer Therapeutic Effect by Inhibiting TNF-α-Induced NF-κB Activation
Wang, Z., Li, M.-Y., Mi, C., Wang, K.-S., Ma, J., & Jin, X.-J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081619 · Cited by 32
WNT/β-catenin pathway modulates the TNF-α-induced inflammatory response in bronchial epithelial cells.
Jang, J., Jung, Y., Chae, S., Chung, S.-I., Kim, S.-M., & Yoon, Y. (2017) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2017.01.156 · Cited by 32
“It is well-known that TNF-a activates intracellular signaling events leading to phosphorylation of IkB followed by its degradation, which frees NF-kB for translocation into the nucleus [3,6].”
Background
Schizandrin C regulates lipid metabolism and inflammation in liver fibrosis by NF-κB and p38/ERK MAPK signaling pathways
Chen, P., Wang, R., Liu, F., Li, S., Gu, Y., Wang, L., & Yuan, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1092151 · Cited by 23
Anti-inflammatory therapy of atherosclerosis: focusing on IKKβ
Gan, J., Guo, L., Zhang, X., Yu, Q., Yang, Q., Zhang, Y., Zeng, W., Jiang, X., & Guo, M. (2023) · Journal of Inflammation · doi:10.1186/s12950-023-00330-5 · Cited by 38
“TNF-α, IL-1, and LPS all fail to activate NF-κB [38].”
Background
Copper homeostasis and the ubiquitin proteasome system
Zhang, B., & Burke, R. (2023) · Metallomics · doi:10.1093/mtomcs/mfad010 · Cited by 36
Intersection of the Ubiquitin–Proteasome System with Oxidative Stress in Cardiovascular Disease
Qiu, M., Chen, J., Li, X., & Zhuang, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012197 · Cited by 43
Cynarin attenuates LPS-induced endothelial inflammation via upregulation of the negative regulator MKP-3
Kim, D. B., Unenkhuu, B., Kim, G. J., Kim, S.-W., & Kim, H. S. (2022) · Animal Cells and Systems · doi:10.1080/19768354.2022.2077438 · Cited by 33
“Extracellular proinflammatory stimuli cause IκB to be phosphorylated and degraded; as a result, free NF-κB is translocated to the nucleus, stimulating the expression of downstream genes (Karin and Ben-Neriah 2000).”
Background
Integrative Proteomic Analysis of Multiple Posttranslational Modifications in Inflammatory Response
Ji, F., Zhou, M., Zhu, H., Jiang, Z., Li, Q., Ouyang, X., Lv, Y., Zhang, S., Wu, T., & Li, L. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2020.11.004 · Cited by 37
“Phosphorylation is a widely investigated type of PTMs in innate immunity [4].”
In vivo assessment of molybdenum and cadmium co-induced the mRNA levels of heat shock proteins, inflammatory cytokines and apoptosis in shaoxing duck (Anas platyrhyncha) testicles
Dai, X., Nie, G., Cao, H., Xing, C., Hu, G., & Zhang, C. (2019) · Poultry Science · doi:10.3382/ps/pez328 · Cited by 33
Nitrated fatty acids: from diet to disease
Khoo, N., & Schopfer, F. (2019) · Current Opinion in Physiology · doi:10.1016/j.cophys.2019.04.013 · Cited by 31
Pyrrolidine Dithiocarbamate (PDTC) Inhibits DON-Induced Mitochondrial Dysfunction and Apoptosis via the NF-κB/iNOS Pathway
Wan, D., Wu, Q.-H., Qu, W., Liu, G., & Wang, X. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1324173 · Cited by 31
Biomarkers in abnormal uterine bleeding†
Chodankar, R., & Critchley, H. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy231 · Cited by 31
“The canonical pathway is triggered by microbial products and proinflammatory cytokines such as TNFα and IL-1, while the alternative pathway is triggered by TNF-family cytokines but not TNFα [51, 52].”
BackgroundInfluential
Isolation of Novel Sesquiterpeniods and Anti-neuroinflammatory Metabolites from Nardostachys jatamansi
Yoon, C.-S., Kim, D.-C., Park, J.-S., Kim, K.-W., Kim, Y.-C., & Oh, H. (2018) · Molecules · doi:10.3390/molecules23092367 · Cited by 31
“Therefore, suppression of the NF-κB pathway is a widely used strategy for inhibiting neuroinflammation [21,22].”
Method
BHDPC Is a Novel Neuroprotectant That Provides Anti-neuroinflammatory and Neuroprotective Effects by Inactivating NF-κB and Activating PKA/CREB
Li, C., Chen, T., Zhou, H., Feng, Y., Hoi, M. P. M., Ma, D., Zhao, C., Zheng, Y., & Lee, S. M. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00614 · Cited by 32
“The activated microglia-mediated neuroinflammatory responses are characterized by pro-inflammatory molecule production, which is well known to be regulated by the transcription factor NF-κB signaling pathway (Baeuerle and Henkel, 1994; Karin and Ben-Neriah, 2000).”
Background
Roburic Acid Suppresses NO and IL-6 Production via Targeting NF-κB and MAPK Pathway in RAW264.7 Cells
Chen, Y.-F., Ji, N., Pan, S., Zhang, Z., Wang, R., Qiu, Y.-L., Jin, M.-H., & Kong, D. (2017) · Inflammation · doi:10.1007/s10753-017-0636-z · Cited by 31
Integrating novel drugs to chemoimmunotherapy in diffuse large B-cell lymphoma
Chiappella, A., Santambrogio, E., Castellino, A., Nicolosi, M., & Vitolo, U. (2017) · Expert Review of Hematology · doi:10.1080/17474086.2017.1350164 · Cited by 31
Influence of Different Light Spectra on Melatonin Synthesis by the Pineal Gland and Influence on the Immune System in Chickens
Horodincu, L., & Solcan, C. (2023) · Animals · doi:10.3390/ani13132095 · Cited by 38
A novel hypothesis for COVID-19 pathogenesis: Retinol depletion and retinoid signaling disorder
Sarohan, A. R., Kızıl, M., İnkaya, A. Ç., Mahmud, S. O., Akram, M., & Çen, O. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110121 · Cited by 44
Challenges with Methods for Detecting and Studying the Transcription Factor Nuclear Factor Kappa B (NF-κB) in the Central Nervous System
Mostafizar, M., Cortes-Pérez, C. M., Snow, W. M., Djordjevic, J., Adlimoghaddam, A., & Albensi, B. C. (2021) · Cells · doi:10.3390/cells10061335 · Cited by 36
“For example, NF-κB subunits are not exclusively localized in the nucleus of a cell [64], and NF-κB signaling involves several steps, as follow: the activation of IKK [65], IκB degradation [66] and ubiquitination [67], post-translational modification of the NF-κB subunits [68,69], and translocation of the NF-κB dimers…”
San Wu Huangqin decoction regulates inflammation and immune dysfunction induced by influenza virus by regulating the NF-κB signaling pathway in H1N1-infected mice.
Ma, Q.-H., Ren, M.-Y., & Luo, J.-B. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112800 · Cited by 30
Curdlan (Alcaligenes faecalis) (1→3)-β-d-Glucan Oligosaccharides Drive M1 Phenotype Polarization in Murine Bone Marrow-Derived Macrophages via Activation of MAPKs and NF-κB Pathways
Liu, J., Tang, J., Li, X., Yan, Q., Ma, J.-W., & Jiang, Z.-Q. (2019) · Molecules · doi:10.3390/molecules24234251 · Cited by 30
“In the innate immune system of the host, NO could serve as the killer of infected cells, tumor cells, and parasitic pathogens [37].”
Background
Eupatilin attenuates the inflammatory response induced by intracerebral hemorrhage through the TLR4/MyD88 pathway
Fei, X., Chen, C., Kai, S., Fu, X., Man, W., Ding, B., Wang, C., & Xu, R. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.105837 · Cited by 33
Centaurium erythraea extract improves survival and functionality of pancreatic beta-cells in diabetes through multiple routes of action
Đorđević, M., Grdović, N., Mihailović, M., Јovanović, J. A., Uskoković, A. S., Rajić, J., Đorđević, M., Tolić, A., Mišić, D. M., Šiler, B., et al. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.112043 · Cited by 32
Synthesis of new ent-labdane diterpene derivatives from andrographolide and evaluation of their anti-inflammatory activities.
Wang, W., Wu, Y., Chen, X., Zhang, P., Li, H., & Chen, L.-X. (2019) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2018.11.002 · Cited by 30
Recombinant fibromodulin and decorin effects on NF-κB and TGFβ1 in the 4T1 breast cancer cell line.
Nejad, L. D., Biglari, A., Annese, T., & Ribatti, D. (2017) · Oncology Letters · doi:10.3892/ol.2017.5960 · Cited by 30
“In response to certain stimulatory agents, including viral infection, inflammatory cytokines and bacterial lipopolysaccharide, I κ Bs are rapidly phosphorylated and degraded to promote the nuclear transfer of NF-κ B and the activation of a number of genes (34,35).”
MicroRNA‐3178 ameliorates inflammation and gastric carcinogenesis promoted by Helicobacter pylori new toxin, Tip‐α, by targeting TRAF3
Zou, M.-J., Wang, F., Jiang, A.-Q., Xia, A.-L., Kong, S., Gong, C.-S., Zhu, M.-X., Zhou, X., Zhu, J., Zhu, W.-G., et al. (2017) · Helicobacter · doi:10.1111/hel.12348 · Cited by 30
Rho kinase inhibition ameliorates cyclophosphamide-induced cystitis in rats
Wróbel, A., Doboszewska, U., Rechberger, E., Rojek, K., Serefko, A., Poleszak, E., Skalicka-Wożniak, K., Dudka, J., & Wlaź, P. (2017) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-017-1361-8 · Cited by 30
“It was shown that pre-treatment with antiTNF-α or anti-IL-1β serum diminished mucosal erosion, hemorrhage, edema, leukocyte migration, and ulceration in CYP-injected mice (Gomes et al. 1995).”
BackgroundInfluential
Association of NFKB1 gene polymorphism (rs28362491) with levels of inflammatory biomarkers and susceptibility to diabetic nephropathy in Asian Indians
Gautam, A., Gupta, S., Mehndiratta, M., Sharma, M., Singh, K., Kalra, O. P., Agarwal, S., & Gambhir, J. (2017) · World Journal of Diabetes · doi:10.4239/wjd.v8.i2.66 · Cited by 30
Progress on innate immune evasion and live attenuated vaccine of pseudorabies virus
Nie, Z., Zhu, S., Wu, L., Sun, R., Shu, J., He, Y., & Feng, H. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1138016 · Cited by 32
Neuroprotective effects of roflumilast against quinolinic acid-induced rat model of Huntington’s disease through inhibition of NF-κB mediated neuroinflammatory markers and activation of cAMP/CREB/BDNF signaling pathway
Saroj, P., Bansal, Y., Singh, R., Akhtar, A., Sodhi, R. K., Bishnoi, M., Sah, S. P., & Kuhad, A. (2021) · Inflammopharmacology · doi:10.1007/s10787-020-00787-3 · Cited by 32
Sodium propionate protect the blood-milk barrier integrity, relieve lipopolysaccharide-induced inflammatory injury and cells apoptosis
Ali, I., Yang, M., Wang, Y., Yang, C., Shafiq, M., Wang, G., & Li, L. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119138 · Cited by 29
The NLRP3 inflammasome: a therapeutic target for inflammation-associated cancers
Gouravani, M., Khalili, N., Razi, S., Keshavarz‐Fathi, M., Khalili, N., & Rezaei, N. (2020) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2020.1713755 · Cited by 33
The involvement of NF-κB/P38 pathways in Scutellaria baicalensis extracts attenuating of Escherichia coli K88-induced acute intestinal injury in weaned piglets
Huang, C.-Y., Wang, Y., He, X., Jiao, N., Zhang, X., Qiu, K., Piao, X., & Yin, J.-D. (2019) · British Journal of Nutrition · doi:10.1017/s0007114519000928 · Cited by 29
Cellular and Molecular Mechanisms Underlying Arterial Baroreceptor Remodeling in Cardiovascular Diseases and Diabetes
Tu, H., Zhang, D., & Li, Y. (2018) · Neuroscience Bulletin · doi:10.1007/s12264-018-0274-y · Cited by 31
Glycogen synthase kinase 3 (GSK3) inhibition: a potential therapeutic strategy for Alzheimer’s disease
Karati, D., Meur, S., Roy, S., Mukherjee, S., Debnath, B., Jha, S. K., Sarkar, B. K., Naskar, S., & Ghosh, P. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03500-1 · Cited by 31
“Two important kinases, IKKα and IKKβ, compose the catalytic domains of the IκB kinase (IKK) complex (Karin and Ben-Neriah 2000; Medunjanin et al. 2016).”
Advances in molecular mechanisms of inflammatory bowel disease‑associated colorectal cancer (Review)
Wang, Z., Chang, Y., Sun, H., Li, Y., & Tang, T. (2024) · Oncology Letters · doi:10.3892/ol.2024.14390 · Cited by 34
“This activity is similar to the function of IKKβ in myeloid cells.”
Influential
Exploring sulforaphane as neurotherapeutic: targeting Nrf2-Keap & Nf-Kb pathway crosstalk in ASD
Shah, A., Varma, M., & Bhandari, R. (2023) · Metabolic brain disease · doi:10.1007/s11011-023-01224-4 · Cited by 28
“The IκBs mask the nuclear localization sequences of NF-κB and create problems with recognition of the NF-κB nuclear localization signal (NLS) by the nuclear import machinery, as a result retaining NF-κB in the cytoplasm (Karin and Ben-Neriah 2000).”
β-Nicotinamide Mononucleotide (NMN) Administrated by Intraperitoneal Injection Mediates Protection Against UVB-Induced Skin Damage in Mice
Zhou, X., Du, H.-H., Long, X., Pan, Y., Hu, J. P., Yu, J., & Zhao, X. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s327329 · Cited by 29
Sarcopenia versus cancer cachexia: the muscle wasting continuum in healthy and diseased aging
Moreira‐Pais, A., Ferreira, R. M., Oliveira, P. A., & Duarte, J. A. (2021) · Biogerontology · doi:10.1007/s10522-021-09932-z · Cited by 31
Fine Particulate Matter (PM2.5) upregulates expression of Inflammasome NLRP1 via ROS/NF-κB signaling in HaCaT Cells
Dong, L., Hu, R., Yang, D., Zhao, J., Kan, H., Tan, J., Guan, M., Kang, Z., & Xu, F. (2020) · International Journal of Medical Sciences · doi:10.7150/ijms.46962 · Cited by 27
“NF-κB-mediated gene expression can also regulate the production of inflammatory mediators [25].”
Background
Role of Chondrocytes in the Development of Rheumatoid Arthritis Via Transmembrane Protein 147–Mediated NF ‐κB Activation
Ota, M., Tanaka, Y., Nakagawa, I., Jiang, J., Arima, Y., Kamimura, D., Onodera, T., Iwasaki, N., & Murakami, M. (2019) · Arthritis & Rheumatology · doi:10.1002/art.41182 · Cited by 35
Innate Immunity and Alcohol
Kany, S., Janicova, A., & Relja, B. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8111981 · Cited by 39
“IKK phosphorylates IkB, thus exposing it to disassembly via ubiquitination [36].”
Background
HSP70/DNAJA3 chaperone/cochaperone regulates NF-κB activity in immune responses.
Kumada, K., Fuse, N., Tamura, T., Okamori, C., & Kurata, S. (2019) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2019.04.077 · Cited by 28

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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