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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Background
Zhilong Huoxue Tongyu Capsules Ameliorate Early Brain Inflammatory Injury Induced by Intracerebral Hemorrhage via Inhibition of Canonical NFкβ Signalling Pathway
Mazhar, M., Yang, G., Mao, L., Liang, P., Tan, R., Wang, L., Xu, H., Yang, L., Ren, W., & Yang, S. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.850060 · Cited by 25
“The canonical pathway is triggered by proinflammatory cytokines such as TNFα and IL1 (Karin and Ben-Neriah, 2000) derived from astrocytes, neurons and majorly microglia/macrophages (Wang et al., 2011b).”
BackgroundInfluential
Insights Into Genome-Wide Association Study for Diabetes: A Bibliometric and Visual Analysis From 2001 to 2021
Liu, Y., Wang, Y., Qin, S., Jin, X., Jin, L., Gu, W., & Mu, Y. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.817620 · Cited by 20
“In addition, TNFRSF4 and MAP3K2 are involved in the activation of nuclear factor kappa B (NF-kB) (51).”
Background
DNA Methylation Malleability and Dysregulation in Cancer Progression: Understanding the Role of PARP1
Srivastava, R., & Lodhi, N. (2022) · Biomolecules · doi:10.3390/biom12030417 · Cited by 22
Cytokine induced 3‐D organotypic psoriasis skin model demonstrates distinct roles for NF‐κB and JAK pathways in disease pathophysiology
Todorović, V., McDonald, H. A., Hoover, P., Wetter, J. B., Marinopoulos, A. E., Woody, C. L., Miller, L. N., Finkielsztein, A., Dunstan, R. W., Paller, A. S., et al. (2022) · Experimental Dermatology · doi:10.1111/exd.14551 · Cited by 20
13,13a-seco-protoberberines from the tubers of Corydalis yanhusuo and their anti-inflammatory activity.
Xia, G.-Y., Fang, D.-J., Wang, L., Xia, H., Wang, Y.-N., Shang, H.-C., & Lin, S. (2021) · Phytochemistry · doi:10.1016/j.phytochem.2021.113023 · Cited by 19
The NF-κB Pathway: Modulation by Entamoeba histolytica and Other Protozoan Parasites
Chadha, A., & Chadee, K. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.748404 · Cited by 19
“The phosphorylation of IkB at N-terminal Ser 32 and Ser 36 (Karin and Ben-Neriah, 2000), mediated by IKK, leads to Frontiers in Cellular and Infection Microbiology | www.frontiersin.org 3 proteasomal degradation of the inhibitory subunit by 26S proteasome, resulting in NF-kB activation.…”
Background
Genetic Events Inhibiting Apoptosis in Diffuse Large B Cell Lymphoma
Léveillé, E., & Johnson, N. A. (2021) · Cancers · doi:10.3390/cancers13092167 · Cited by 26
“This leads to formation of the CARD11-BCL10-MALT1 (CBM) complex, which allows translocation of cytoplasmic NF-kB to the nucleus to facilitate target gene transcription [132-134].”
Background
In vitro anti-inflammatory potential of marine macromolecules cross-linked bio-composite scaffold on LPS stimulated RAW 264.7 macrophage cells for cartilage tissue engineering applications
Sumayya, A. S., & Kurup, G. M. (2021) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2021.1899590 · Cited by 27
Anti-inflammatory properties of the ethanol extract from Clerodendrum cyrtophyllum Turcz based on in vitro and in vivo studies.
Nguyen, T. H., Nachtergael, A., Nguyen, T. M., Cornet, V., Duez, P., Muller, M., Duong, H., & Kestemont, P. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112739 · Cited by 19
“…from a complex with I-κB, now becoming enabled to migrate to the nucleus where it binds to the cisacting κB enhancer element of target genes and induces transcription of its target genes such as COX-2, iNOS, TNF-α, IL-1β, and IL-6, chemokines and adhesion molecules (Karin and Ben-neriah, 2000).”
Background
The NF-κB family member dorsal plays a role in immune response against Gram-positive bacterial infection in mud crab (Scylla paramamosain).
Deng, H., Hu, L., Li, J.-J., Yan, W., Song, E.-H., Kuang, M., Liu, S., He, J.-G., & Weng, S. (2019) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2019.103581 · Cited by 19
Targeting the KRAS, p38α, and NF‐κB in lung adenocarcinoma cancer cells: The effect of combining RNA interferences with a chemical inhibitor
Zarredar, H., Pashapour, S., Farajnia, S., Ansarin, K., Baradaran, B., Ahmadzadeh, V., & Safari, F. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28357 · Cited by 19
An Algal Metabolite-Based PPAR-γ Agonist Displayed Anti-Inflammatory Effect via Inhibition of the NF-κB Pathway
Ju, Z.-R., Su, M., Li, D.-D., Hong, J., Im, D., Kim, S., Kim, E. L., & Jung, J. H. (2019) · Marine Drugs · doi:10.3390/md17060321 · Cited by 19
Cyanidin-3-o-β-Glucoside Induces Megakaryocyte Apoptosis via PI3K/Akt- and MAPKs-Mediated Inhibition of NF-κB Signalling
Ya, F.-L., Li, Q., Wang, D.-L., Xie, S.-F., Song, F., Gallant, R. C., Tian, Z., Wan, J.-B., Ling, W., & Yang, Y. (2018) · Thrombosis and Haemostasis · doi:10.1055/s-0038-1656551 · Cited by 19
Trichomonas vaginalis Induces SiHa Cell Apoptosis by NF-κB Inactivation via Reactive Oxygen Species
Quan, J.-H., Kang, B.-H., Yang, J.-B., Rhee, Y., Noh, H., Choi, I.-W., Cha, G.-H., Yuk, J., & Lee, Y.-H. (2017) · BioMed Research International · doi:10.1155/2017/3904870 · Cited by 19
N-Myc-Interacting Protein Negatively Regulates TNF-α-Induced NF-κB Transcriptional Activity by Sequestering NF-κB/p65 in the Cytoplasm
Hou, J.-J., Jiang, S., Zhao, J.-B., Zhu, D., Zhao, X., Cai, J.-C., & Zhang, S.-Q. (2017) · Scientific Reports · doi:10.1038/s41598-017-15074-5 · Cited by 19
5-Aminosalicylic acid inhibits inflammatory responses by suppressing JNK and p38 activity in murine macrophages
Qu, T.-L., Wang, E., Jin, B., Li, W.-P., Liu, R.-L., & Zhao, Z.-B. (2017) · Immunopharmacology and immunotoxicology · doi:10.1080/08923973.2016.1274997 · Cited by 19
Biomimetic mineralized mesenchymal stem cell-derived exosomes for dual modulation of ferroptosis and lactic acid-driven inflammation in acute liver injury therapy.
Tian, Y., Zhang, J., Jia, Z., Pan, X.-H., Hu, Z., Kang, R.-X., Zhou, X., Luo, L., Shen, Z.-Q., & Shen, Q. (2025) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2025.02.078 · Cited by 18
Anti-Inflammatory Response of New Postbiotics in TNF-α/IFN-γ-Induced Atopic Dermatitis-like HaCaT Keratinocytes
Kim, Y.-K., Cho, M., & Kang, D.-J. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46060364 · Cited by 18
Affected inflammation-related signaling pathways in snake envenomation: A recent insight.
Luo, P., Ji, Y., Liu, X., Zhang, W., Cheng, R., Zhang, S., Qian, X., & Huang, C.-H. (2023) · Toxicon · doi:10.1016/j.toxicon.2023.107288 · Cited by 18
Phenylalanine Plays Important Roles in Regulating the Capacity of Intestinal Immunity, Antioxidants and Apoptosis in Largemouth Bass (Micropterus salmoides)
Yi, C., Liang, H.-L., Huang, D.-Y., Yu, H., Xue, C.-Y., Gu, J.-Z., Chen, X.-R., Wang, Y., Ren, M.-C., & Zhang, L. (2023) · Animals · doi:10.3390/ani13182980 · Cited by 18
Estrogen Receptor-α Targeting: PROTACs, SNIPERs, Peptide-PROTACs, Antibody Conjugated PROTACs and SNIPERs
Negi, A., Kesari, K. K., & Voisin‐Chiret, A. S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14112523 · Cited by 18
“The peptidic character of IκBα limits its cellular penetrability and requires phosphorylation on two serine residues to be recognized by SCFβ−TRCP, making it susceptive to phosphatases [74].”
Background
Modulation of Inflammation by Plant-Derived Nutraceuticals in Tendinitis
Mueller, A., Brockmueller, A., Kunnumakkara, A. B., & Shakibaei, M. (2022) · Nutrients · doi:10.3390/nu14102030 · Cited by 25
“Under resting conditions, NF-κB is located as a heterodimeric complex consisting of p50 and p65 in a latent state in the cytoplasm, bound to its natural inhibitor nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha (IκBα) [83,84].”
Background
Anti-Inflammatory Extract from Soil Algae Chromochloris zofingiensis Targeting TNFR/NF-κB Signaling at Different Levels
Leitner, P. D., Jakschitz, T., Gstir, R., Stuppner, S., Perkams, S., Kruus, M., Trockenbacher, A., Griesbeck, C., Bonn, G., Huber, L. A., et al. (2022) · Cells · doi:10.3390/cells11091407 · Cited by 18
The Kynurenine Pathway and Polycystic Ovary Syndrome: Inflammation as a Common Denominator
Jovanović, F., Sudhakar, A., & Knežević, N. N. (2022) · International Journal of Tryptophan Research · doi:10.1177/11786469221099214 · Cited by 23
Impact of a long-term high-glucose environment on pro-inflammatory responses in macrophages stimulated with lipopolysaccharide
Suzuki, T., Yamashita, S., Hattori, K., Matsuda, N., & Hattori, Y. (2021) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-021-02137-8 · Cited by 18
Triptolidenol, isolated from Tripterygium wilfordii, disrupted NF-κB/COX-2 pathway by targeting ATP-binding sites of IKKβ in clear cell renal cell carcinoma.
Jin, J., Zhou, M.-R., Wang, X., Liu, M., Huang, H.-L., Yan, F., Yu, Z., Shu, X.-H., Huo, X.-K., Feng, L., et al. (2020) · Fitoterapia · doi:10.1016/j.fitote.2020.104779 · Cited by 18
The link “Cancer and autoimmune diseases” in the light of microbiota: Evidence of a potential culprit
Niccolai, E., Boem, F., Emmi, G., & Amedei, A. (2020) · Immunology Letters · doi:10.1016/j.imlet.2020.03.001 · Cited by 23
Therapeutic Effects of Curcumin against Bladder Cancer: A Review of Possible Molecular Pathways.
Ashrafizadeh, M., Yaribeygi, H., & Sahebkar, A. (2020) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520620666200203143803 · Cited by 18
Anti-tumor mechanism of eicosapentaenoic acid (EPA) on ovarian tumor model by improving the immunomodulatory activity in F344 rats
Bie, N., Han, L.-R., Meng, M., Zhang, Y., Guo, M.-Z., & Wang, C.-L. (2020) · doi:10.1016/j.jff.2019.103739 · Cited by 18
Identification and functional characterization of the transcription factor NF-κB subunit p65 in common carp (Cyprinus carpio L.).
Shan, S., Liu, R.-R., Feng, H., Zhang, Y.-H., Zhang, F.-M., Lv, C., & Yang, G.-W. (2019) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2019.10.014 · Cited by 18
Paraffin-embedding lithography and micro-dissected tissue micro-arrays: tools for biological and pharmacological analysis of ex vivo solid tumors.
Simeone, K., Guay-Lord, R., Lateef, M. A., Péant, B., Kendall-Dupont, J., Orimoto, A., Carmona, E., Provencher, D., Saad, F., Gervais, T., et al. (2019) · Lab on a Chip · doi:10.1039/c8lc00982a · Cited by 18
Genome-wide DNA methylation patterns in coronary heart disease
Wang, X., Liu, A.-H., Jia, Z., Pu, K., Chen, K.-Y., & Guo, H. (2017) · Herz · doi:10.1007/s00059-017-4616-8 · Cited by 19
Effects of mycoplasma infection on the host organism response via p53/NF‐κB signaling
Borchsenius, S. N., Daks, A. A., Fedorova, O., Chernova, O. A., & Barlev, N. A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26781 · Cited by 27
Delayed xenon post-conditioning mitigates spinal cord ischemia/reperfusion injury in rabbits by regulating microglial activation and inflammatory factors
Yang, Y.-W., Wang, Y.-L., Lu, J.-K., Tian, L., Jin, M., & Cheng, W.-P. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.228757 · Cited by 18
“It is well known that necrosis and apoptosis can coexist in SCI (Karin and Ben-Neriah, 2000).”
Background
Ubiquitin C‐terminal hydrolase‐L3 promotes interferon antiviral activity by stabilizing type I‐interferon receptor
Zhao, P., Guo, T.-T., Qian, L.-P., Wang, X.-F., Yuan, Y.-K., Cheng, Q., Zuo, Y.-B., Liu, J., Miao, Y., Feng, Q., et al. (2017) · Antiviral Research · doi:10.1016/j.antiviral.2017.06.002 · Cited by 18
“SCF TrCP E3 ligases can induce ubiquitination and degradation of phosphorylated substrates including (IkB) (Kanarek and Ben-Neriah, 2012; Karin and Ben-Neriah, 2000), b-catenin (Noubissi et al.”
Background
Immune defects caused by mutations in the ubiquitin system
Etzioni, A., Ciechanover, A. J., & Pikarsky, E. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.11.031 · Cited by 17
Differential proteomics analysis of Frankliniella occidentalis immune response after infection with Tomato spotted wilt virus (Tospovirus)
Ogada, P. A., Kiirika, L. M., Lorenz, C., Senkler, J., Braun, H., & Poehling, H. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.10.013 · Cited by 15
Combined Parthenolide and Balsalazide Have Enhanced Antitumor Efficacy Through Blockade of NF-κB Activation
Kim, S.-L., Kim, S., Park, Y. R., Liu, Y.-C., Kim, E.-M., Jeong, H.-J., Kim, Y. N., Seo, S., Kim, I., Lee, S.-O., et al. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0101 · Cited by 18
“IKK phosphorylates NF-kB–bound IkBs and targets them for ubiquitindependent degradation, allowing liberated NF-kB dimers to enter the nucleus (47).”
Background
A sirtuin activator and an anti-inflammatory molecule—multifaceted roles of adjudin and its potential applications for aging-related diseases
Xia, W., & Geng, K. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.020 · Cited by 19
Differential regulatory mechanisms of gut-derived SCFAs (acetate, propionate, butyrate) on the pulmonary TLR2 signaling pathway and their roles in the inflammatory balance of bacterial pneumonia
Chen, H., Xu, Y., Qiu, J.-L., Guan, Z.-W., Yu, S.-P., & Ding, Y. (2026) · European Journal of Medical Research · doi:10.1186/s40001-025-03666-1 · Cited by 17
PRRSV-2 nsp2 Ignites NLRP3 inflammasome through IKKβ-dependent dispersed trans-Golgi network translocation
Zhang, L., Gao, Y., Zhou, H., Liang, X. H., Jiang, X., Gong, W., Sun, Y., Zhang, D., Wang, X., Nauwynck, H., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012915 · Cited by 18
“Once the serine on the activation loop of IKK β is mutated to alanine, TNF-α , IL-1, and LPS all fail to activate NF-κ B [12].”
Interplay between SUMO1-related SUMOylation and phosphorylation of p65 promotes hepatocellular carcinoma progression.
Jiang, C., Zhang, C., Dai, M., Wang, F., Xu, S., Han, D., Wang, Y., Cao, Y.-J., Liang, Y., Zhang, Z., et al. (2023) · Biochimica et biophysica acta. Molecular cell research · doi:10.1016/j.bbamcr.2023.119595 · Cited by 17
MiR-196b-5p activates NF-κB signaling in non-small cell lung cancer by directly targeting NFKBIA
Zhu, W., Yu, Y., Ye, Y., Tu, X., Zhang, Y., Wu, T., Ni, L., Huang, X., Wang, Y., & Cui, R. (2023) · Translational Oncology · doi:10.1016/j.tranon.2023.101755 · Cited by 16
“NFKBIA, also known as IκBα, is a member of IkBs that negatively regulates NF-κB signaling [15].”
BackgroundInfluential
Surfactin-oleogel with therapeutic potential for inflammatory acne vulgaris induced by Propionibacterium acnes
Shan, M., Meng, F.-Q., Tang, C., Zhou, L.-B., Lu, Z., & Lu, Y. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11719-8 · Cited by 17
“When stimulated by inflammatory factors, IκBα will be phosphorylated and degraded, and two dimers of NF-κB will be released into the cell nucleus, and then NF-κB is activated (Karin and Ben-Neriah 2000).”
Background
TICAM-1/TRIF associates with Act1 and suppresses IL-17 receptor–mediated inflammatory responses
Miyashita, Y., Kouwaki, T., Tsukamoto, H., Okamoto, M., Nakamura, K., & Oshiumi, H. (2021) · Life Science Alliance · doi:10.26508/lsa.202101181 · Cited by 17
“…et al. https://doi.org/10.26508/lsa.202101181 vol 5 | no 2 | e202101181 4 of 14 TICAM-1 is a negative regulator of IL-17RA signaling Miyashita et al. https://doi.org/10.26508/lsa.202101181 vol 5 | no 2 | e202101181 5 of 14 is a hallmark of NF-κB pathway activation (Karin & Ben-Neriah, 2000).”
BackgroundInfluential
Late p65 nuclear translocation in glioblastoma cells indicates non-canonical TLR4 signaling and activation of DNA repair genes
Moretti, I. F., Lerário, A., Trombetta-Lima, M., Sola, P., Soares, R. D. S., Oba-Shinjo, S., & Marie, S. K. N. (2021) · Scientific Reports · doi:10.1038/s41598-020-79356-1 · Cited by 17
Ubiquitination modification: critical regulation of IRF family stability and activity
Liu, B., Jin, J., & Li, Y. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1796-0 · Cited by 23
Cynanchum paniculatum and Its Major Active Constituents for Inflammatory-Related Diseases: A Review of Traditional Use, Multiple Pathway Modulations, and Clinical Applications
Chen, J.-X., Cheng, C.-S., Chen, J., Lv, L., Chen, Z.-X., Chen, C., & Zheng, L. (2020) · Evidence-Based Complementary and Alternative Medicine · doi:10.1155/2020/7259686 · Cited by 17
Exploring Inhibitory Mechanisms of Green Tea Catechins as Inhibitors of a Cancer Therapeutic Target, Nuclear Factor-κB (NF-κB)
Suhail, M., Parveen, A., Husain, A., & Rehan, M. (2019) · Biosciences Biotechnology Research Asia · doi:10.13005/bbra/2787 · Cited by 17
Sinomenine relieves oxygen and glucose deprivation-induced microglial activation via inhibition of the SP1/miRNA-183-5p/IκB-α signaling pathway.
Qin, F., Zhao, Y., Shang, W., Zhao, Z.-M., Qian, X., Zhang, B., & Cai, H. (2018) · Cellular and Molecular Biology · doi:10.14715/cmb/2018.64.10.23 · Cited by 17
“In the classic NF-κB pathway, various pathogens, including reactive oxygen species, endotoxin, bacterial tumor necrosis factor alpha, etc, are considered as common stimuli for incurable inflammation (14).”
Background
Importins α and β Signaling Mediates Endothelial Cell Inflammation and Barrier Disruption
Leonard, A., Rahman, A., & Fazal, F. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.01.011 · Cited by 17
Pyrrolidine dithiocarbamate ameliorates endothelial dysfunction in thoracic aorta of diabetic rats by preserving vascular DDAH activity
Lu, C.-W., Lin, Y., Lei, Y., Wang, L., He, Z.-M., & Xiong, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179908 · Cited by 17
Regulation of NLRP3/TRIM family signaling in gut inflammation and colorectal cancer
Mohapatra, B. S., Lavudi, K., Kokkanti, R. R., & Patnaik, S. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189271 · Cited by 16
Ethanol extract of lymphanax with gypenoside 17 and ginsenoside Re exerts anti-inflammatory properties by targeting the AKT/NF-κB pathway
Choi, W.-S., Kim, H. S., Kim, D., Hong, Y.-D., Kim, H.-J., Kim, J. H., Kim, J.-H., & Cho, J. Y. (2024) · Journal of Ginseng Research · doi:10.1016/j.jgr.2024.08.003 · Cited by 16
Nimbolide Targets Multiple Signalling Pathways to Reduce Neuroinflammation in BV-2 Microglia
Katola, F. O., & Olajide, O. A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03410-y · Cited by 16
TJ-M2010-5, a novel CNS drug candidate, attenuates acute cerebral ischemia-reperfusion injury through the MyD88/NF-κB and ERK pathway
Li, Z., Zhao, M., Zhang, X., Lu, Y., Yang, Y., Xie, Y., Zou, Z., Zhou, L., Shang, R., Zhang, L., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1080438 · Cited by 17
“IκB kinases (IKKs) act immediately after TLR4/MyD88 signaling to phosphorylate IκB and NF-κB p65, which results in the degradation of IκB and nuclear translocation of NF-κB p65 (Karin and Ben-Neriah, 2000).”
Background
Enhanced stability of M1 protein mediated by a phospho-resistant mutation promotes the replication of prevailing avian influenza virus in mammals
Wang, C., Qu, R., Zong, Y., Qin, C., Liu, L., Gao, X., Sun, H., Sun, Y., Chang, K., Zhang, R., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010645 · Cited by 16
“A typical example is the phosphorylation of IκB at S32 and S36 by IκB kinase, which is the signal for ubiquitination and degradation by the proteasome [25].”
Background
Anticancer and Apoptotic Activity in Cervical Adenocarcinoma HeLa Using Crude Extract of Ganoderma applanatum
Kiddane, A. T., Kang, M.-J., Ho, T., Getachew, A., Patil, M., Chun, B.-S., & Kim, G.-D. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44030067 · Cited by 16
“IκB is rapidly phosphorylated, ubiquitinated, and degraded by the proteasome, and the released NFκB dimer is then transferred to the nucleus, where it can regulate specific gene expression [24].”
Background
MAP3K7-IKK Inflammatory Signaling Modulates AR Protein Degradation and Prostate Cancer Progression
Huang, Z., Tang, B., Yang, Y., Yang, Z., Shi, L., Bai, Y., Yan, B., Karnes, R. J., Zhang, J., Jiménez, R. E., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-4194 · Cited by 24
“Increasing evidence indicates that IKK phosphorylation sequences often serve as the phosphodegrons recognized by b-TRCP (39, 40).”
Background
Host Innate Immune Response and Viral Immune Evasion During Alphaherpesvirus Infection
Lum, K. K., & Cristea, I. M. (2020) · Caister Academic Press eBooks · doi:10.21775/9781913652555.07 · Cited by 6
“Relevant to active innate immune signal transduction, cells require the proteasomal degradation of IκB to release the inhibition of NF-κB and promote its translocation into the nucleus (Karin and Ben-Neriah, 2000).”
Background
Effect of nifedipine, a calcium channel blocker, on the generation of nitric oxide and interleukin-1β by murine macrophages activated by lipopolysaccharide from Prevotella intermedia
Choe, S.-H., Choi, E., Hyeon, J.-Y., Keum, B. R., Choi, I. S., & Kim, S. (2020) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-020-01958-3 · Cited by 16
Promotion of osteointegration under diabetic conditions by a silk fibroin coating on 3D-printed porous titanium implants via a ROS-mediated NF-κB pathway
Ma, X.-Y., Ma, T.-C., Feng, Y.-F., Xiang, G., Lei, W., Zhou, D.-P., Yu, H.-L., Xiang, L., & Wang, L. (2020) · Biomedical Materials · doi:10.1088/1748-605x/abaaa1 · Cited by 16
“NF-κ Bp65 then entered into the nucleus, enhancing the transcription of target genes containing pro-inflammatory cytokines, chemokines, and cell-survival genes [34, 48].”
17-Aminogeldanamycin Inhibits Constitutive Nuclear Factor-Kappa B (NF-κB) Activity in Patient-Derived Melanoma Cell Lines
Hartman, M. L., Rogut, M., Mielczarek-Lewandowska, A., Woźniak, M., & Czyż, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113749 · Cited by 16
“In addition, phosphorylation of p65 at Ser 536 is managed in the cytoplasm by a plethora of kinases such as TANK-binding kinase 1 (TBK1), ribosomal kinase 1 (RSK1) and AKT1, in addition to IKK [70–72].”
MSIT: Malonylation Sites Identification Tree
Bao, W., Huang, D.-S., & Chen, Y. (2020) · Current Bioinformatics · doi:10.2174/1574893614666190730110747 · Cited by 19
Simultaneous exposure to vinylcyclohexene and methylmercury in Drosophila melanogaster: biochemical and molecular analyses
Piccoli, B., Segatto, A., Oliveira, C., da Silva, F. D., Aschner, M., & da Rocha, J. B. T. (2019) · BMC Pharmacology and Toxicology · doi:10.1186/s40360-019-0356-0 · Cited by 16
Inhibition of NF‐κB improves sensitivity to irradiation and EGFR‐TKIs and decreases irradiation‐induced lung toxicity
Wang, R., Peng, S., Zhang, X., Wu, Z., Duan, H., Yuan, Y., & Wang, W. (2018) · International Journal of Cancer · doi:10.1002/ijc.31907 · Cited by 17
6-Shogaol reduces progression of experimental endometriosis in vivo and in vitro via regulation of VGEF and inhibition of COX-2 and PGE2-mediated inflammatory responses
Wang, D., Jiang, Y.-L., Yang, X.-X., Wei, Q., & Wang, H.-M. (2018) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2018.22.6.627 · Cited by 16
“Upon activation, NF- Bp65 migrates to the nucleus, eventually leading to the expression and release of several pro-inflammatory cytokines [45-47].”
Background
Presenilin 1 Regulates NF-κB Activation via Association with Breakpoint Cluster Region and Casein Kinase II
Tanaka, Y., Sabharwal, L., Ota, M., Nakagawa, I., Jiang, J., Arima, Y., Ogura, H., Okochi, M., Ishii, M., Kamimura, D., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701446 · Cited by 22
ARD1 contributes to IKKβ-mediated breast cancer tumorigenesis
Zhang, Y., Zhou, H., Tao, Y., Liu, X., Yuan, Z., & Nie, C.-L. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0921-2 · Cited by 16
Dysfunction of cholesterol sensor SCAP promotes inflammation activation in THP-1 macrophages
Ouyang, N., Gan, H., He, Q., Lei, H., Wang, S. Y., Liu, Q., & Zhou, C. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.03.032 · Cited by 14
Y-box protein-associated acidic protein (YBAP1/C1QBP) affects the localization and cytoplasmic functions of YB-1
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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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