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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Fu, D.-X., Kuo, Y.-L., Liu, B.-Y., Jeang, K.-T., & Giam, C.-Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210631200 · Cited by 95
Apoptosis induced by proteasome inhibition in cancer cells: predominant role of the p53/PUMA pathway
Concannon, C. G., Koehler, B. F., Reimertz, C., Murphy, B. M., Bonner, C., Thurow, N., Ward, M. W., Villunger, A., Strasser, A., Kögel, D., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1209974 · Cited by 95
Fibroblast growth factor 21 attenuates hepatic fibrogenesis through TGF-β/smad2/3 and NF-κB signaling pathways
Xu, P., Zhang, Y., Liu, Y., Yuan, Q., Song, L., Liu, M., Liu, Z., Yang, Y., Li, J., Li, D., et al. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.11.012 · Cited by 97
Huang-Lian-Jie-Du Decoction Ameliorates Acute Ulcerative Colitis in Mice via Regulating NF-κB and Nrf2 Signaling Pathways and Enhancing Intestinal Barrier Function
Yuan, Z.-W., Yang, L., Zhang, X.-S., Ji, P., Hua, Y.-L., & Wei, Y.-M. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01354 · Cited by 94
Labdane diterpenoids as potential anti-inflammatory agents
Tran, Q. T. N., Wong, W. S. F., & Chai, C. L. L. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.07.019 · Cited by 112
Anti-inflammatory effects of Phyllanthus amarus Schum. & Thonn. through inhibition of NF-κB, MAPK, and PI3K-Akt signaling pathways in LPS-induced human macrophages
Harikrishnan, H., Jantan, I., Haque, M. A., & Kumolosasi, E. (2018) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-018-2289-3 · Cited by 111
Apoptotic Pathway as the Therapeutic Target for Anticancer Traditional Chinese Medicines
An, W., Lai, H., Zhang, Y., Liu, M., Lin, X., & Cao, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00758 · Cited by 93
“The aberrant expression of NF-κB had been detected in most of cancer cells and the inhibitory κB (IκB) kinases (IKKs) are well recognized as key regulators of the NF-κB pathway (Karin and Ben-Neriah, 2000).”
Background
Chemical constituents of hemp (Cannabis sativa L.) seed with potential anti-neuroinflammatory activity
Zhou, Y., Wang, S., Lou, H., & Fan, P. (2017) · Phytochemistry Letters · doi:10.1016/j.phytol.2017.11.013 · Cited by 105
Impact of Klebsiella pneumoniae in lower gastrointestinal tract diseases
Kaur, C. P., Vadivelu, J., & Chandramathi, S. (2018) · Journal of Digestive Diseases · doi:10.1111/1751-2980.12595 · Cited by 90
Structural Analysis of the Autoinhibition of Ets-1 and Its Role in Protein Partnerships
Garvie, C. W., Pufall, M. A., Graves, B. J., & Wolberger, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206327200 · Cited by 86
Targeting estrogen receptor α for degradation with PROTACs: A promising approach to overcome endocrine resistance
Lin, X., Xiang, H., & Luo, G. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112689 · Cited by 104
Association of NFKB1, which encodes a subunit of the transcription factor NF- B, with alcohol dependence
Edenberg, H. J., Xuei, X., Wetherill, L. F., Bierut, L., Bucholz, K., Dick, D. M., Hesselbrock, V., Kuperman, S., Porjesz, B., Schuckit, M. A., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm368 · Cited by 89
A loop of cancer-stroma-cancer interaction promotes peritoneal metastasis of ovarian cancer via TNFα-TGFα-EGFR
Lau, T.-S., Chan, L. K.-Y., Wong, E. C.-H., Hui, C. W.-C., Sneddon, K., Cheung, T.-H., Yim, S.-F., Lee, J. H.-S., Yeung, C. S.-Y., Chung, T. K.-H., et al. (2017) · Oncogene · doi:10.1038/onc.2016.509 · Cited by 88
The Relationship between Reactive Oxygen Species and the cGAS/STING Signaling Pathway in the Inflammaging Process
Andrade, B., Jara‐Gutiérrez, C., Paz-Araos, M., Vázquez, M. C., Díaz, P., & Murgas, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315182 · Cited by 96
Interferon-Induced Protein 44 Interacts with Cellular FK506-Binding Protein 5, Negatively Regulates Host Antiviral Responses, and Supports Virus Replication
DeDiego, M. L., Nogales, A., Martínez‐Sobrido, L., & Topham, D. J. (2019) · mBio · doi:10.1128/mbio.01839-19 · Cited by 95
“The phosphorylation of IB inhibitors mediated by IKK␤ and IKK␣ leads to their degradation, allowing NF-B to migrate to the nucleus and activate IFN and proinflammatory cytokine expression (10) .”
Vascular aging: Molecular mechanisms and potential treatments for vascular rejuvenation
Mistriotis, P., & Andreadis, S. T. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.05.006 · Cited by 89
Brassica-Derived Plant Bioactives as Modulators of Chemopreventive and Inflammatory Signaling Pathways
Sturm, C., & Wagner, A. E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091890 · Cited by 101
Schistosomal extracellular vesicle‐enclosed miRNAs modulate host T helper cell differentiation
Meningher, T., Barsheshet, Y., Ofir‐Birin, Y., Gold, D., Brant, B., Dekel, E., Sidi, Y., Schwartz, E., Regev‐Rudzki, N., Avni, O., et al. (2019) · EMBO Reports · doi:10.15252/embr.201947882 · Cited by 95
“The regulation of NF-j B activity is mostly post-transcriptional [77]; therefore, we did not expect to find differences in its mRNA level.”
IL-1β and TNFα Differentially Influence NF-κB Activity and FasL-Induced Apoptosis in Primary Murine Hepatocytes During LPS-Induced Inflammation
Rex, J., Lutz, A., Faletti, L. E., Albrecht, U., Thomas, M., Bode, J. G., Borner, C., Sawodny, O., & Merfort, I. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00117 · Cited by 87
“Stimulation with either IL-1β or TNFα activates the IκB kinase (IKK) complex which then mediates phosphorylation, ubiquitination and degradation of IκBs allowing translocation of the free NF-κB dimer into the nucleus to initiate transcription (Karin and Ben-Neriah, 2000).”
Background
Harmine is an inflammatory inhibitor through the suppression of NF-κB signaling
Liu, X., Li, M., Tan, S., Wang, C., Fan, S., & Huang, C. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.05.126 · Cited by 92
Oxidative stress and inflammation in a spectrum of epileptogenic cortical malformations: molecular insights into their interdependence
Arena, A., Zimmer, T. S., van Scheppingen, J., Korotkov, A., Anink, J. J., Mühlebner, A., Jansen, F. E., Hecke, W. V., Spliet, W. G. M., van Rijen, P. C., et al. (2018) · Brain Pathology · doi:10.1111/bpa.12661 · Cited by 89
“© 2018 International Society of Neuropathology 360 neuroinflammation, the accumulation of NF-κB p65 in the nuclei of selected subpopulations of dysmorphic neurons in all pathologies and balloon/giant cells in FCD IIb and TSC suggests that these cells may produce excessive inflammatory mediators via the canonical NF-κB…”
Outer Membrane Vesicles Derived From Escherichia coli Regulate Neutrophil Migration by Induction of Endothelial IL-8
Lee, J., Yoon, Y. J., Kim, J. H., Dinh, N. T. H., Go, G., Tae, S., Park, K., Park, H. T., Lee, C., Roh, T., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02268 · Cited by 92
“Because phosphorylation of the NF-κB inhibitor IκB is a prerequisite for IκB degradation and consequent NF-κB activation (Karin and Ben-Neriah, 2000; Shimada and Rajagopalan, 2010), we treated HMEC-1 with E.”
Method
NEMO Trimerizes through Its Coiled-coil C-terminal Domain
Agou, F., Ye, F., Goffinont, S., Courtois, G., Yamaoka, S., Israël, A., & Véron, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201964200 · Cited by 79
HDAC5 modulates PD-L1 expression and cancer immunity via p65 deacetylation in pancreatic cancer
Zhou, Y., Jin, X., Yu, H., Qin, G.-D., Pan, P., Zhao, J.-Y., Chen, T., Liang, X.-Y., Sun, Y., Wang, B., et al. (2022) · Theranostics · doi:10.7150/thno.69444 · Cited by 78
“Upon phosphorylation, IκB is degraded via the proteasome pathway, liberating NF-κB protein, which then translocated into the nucleus [49, 50].”
Method
Quercetin improves immune function in Arbor Acre broilers through activation of NF-κB signaling pathway
Yang, J.-X., Maria, T. C., Zhou, B., Xiao, F., Wang, M., Mao, Y.-J., & Li, Y. (2020) · Poultry Science · doi:10.1016/j.psj.2019.12.021 · Cited by 78
In Vitro and In Vivo Anti-Inflammatory Effects of Polyphyllin VII through Downregulating MAPK and NF-κB Pathways
Zhang, C., Li, Z., Jia, X., Wang, K., Tu, Y., Wang, R., Liu, K., Lu, T., & He, C. (2019) · Molecules · doi:10.3390/molecules24050875 · Cited by 95
Luteolin-mediated PI3K/AKT/Nrf2 signaling pathway ameliorates inorganic mercury-induced cardiac injury.
Baiyun, R., Li, S.-Y., Liu, B.-Y., Lu, J.-J., Lv, Y.-Y., Xu, J., Wu, J.-H., Li, J.-Y., Lv, Z.-J., & Zhang, Z.-G. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.06.046 · Cited by 76
Influence of Caloric Restriction on Constitutive Expression of NF-κB in an Experimental Mouse Astrocytoma
Mulrooney, T. J., Marsh, J., Urits, I., Seyfried, T. N., & Mukherjee, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018085 · Cited by 75
Hypoxia inducible factor‐1 promotes liver fibrosis in nonalcoholic fatty liver disease by activating PTEN/p65 signaling pathway
Han, J., He, Y., Zhao, H., & Xu, X. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28734 · Cited by 89
NF-κB in the New Era of Cancer Therapy.
Eluard, B., Thieblemont, C., & Baud, V. (2020) · Trends in Cancer · doi:10.1016/j.trecan.2020.04.003 · Cited by 74
Lipopolysaccharide (LPS)-stimulated iNOS Induction Is Increased by Glucosamine under Normal Glucose Conditions but Is Inhibited by Glucosamine under High Glucose Conditions in Macrophage Cells
Hwang, J.-S., Kwon, M.-Y., Kim, K.-H., Lee, Y., Lyoo, I. K., Kim, J. E., Oh, E., & Han, I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737940 · Cited by 86
“This is accompanies NF-κB translocation to the nucleus where the protein activates transcription (21).”
Background
Synthesis, in vitro and in vivo biological evaluation of novel lappaconitine derivatives as potential anti-inflammatory agents
Pang, L., Liu, C., Gong, G.-H., & Quan, Z.-S. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.09.002 · Cited by 72
Cnidilide, an alkylphthalide isolated from the roots of Cnidium officinale , suppresses LPS-induced NO, PGE 2 , IL-1β, IL-6 and TNF-α production by AP-1 and NF-κB inactivation in RAW 264.7 macrophages
Lee, W., Shin, J., Jang, D. S., & Lee, K. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2016.08.021 · Cited by 77
Chronic olanzapine administration causes metabolic syndrome through inflammatory cytokines in rodent models of insulin resistance
Li, H.-Q., Peng, S.-Y., Li, S.-H., Liu, S.-Q., Lv, Y., Yang, N., Yu, L.-Y., Deng, Y.-H., Zhang, Z.-J., Fang, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-36930-y · Cited by 71
A Positive Feedback Loop of AKR1C3-Mediated Activation of NF-κB and STAT3 Facilitates Proliferation and Metastasis in Hepatocellular Carcinoma
Zhou, Q., Tian, W., Jiang, Z., Huang, T., Ge, C., Liu, T., Zhao, F., Chen, T., Cui, Y., Li, H., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2480 · Cited by 112
“Phosphorylated IKKa/b (Ser176/180) was shown to be indispensable for NF-kB activation (20).”
Background
NF-κB signaling in rheumatoid arthritis with focus on fibroblast-like synoviocytes
Samimi, L. N., Farhadi, E., Tahmasebi, M. N., Jamshidi, A., Vaziri, A. S., & Mahmoudi, M. (2020) · Autoimmunity Highlights · doi:10.1186/s13317-020-00135-z · Cited by 80
Research progress on the anticancer effects of vitamin K2
Xv, F., Chen, J.-P., Duan, L., & Li, S.-Z. (2018) · Oncology Letters · doi:10.3892/ol.2018.8502 · Cited by 70
“NF-κ B is a regulatory factor that can be simulated by cytokines to participate in the immune and inflammatory reaction (29).”
In vitro and in vivo anti‐inflammatory effects of theaflavin‐3,3′‐digallate on lipopolysaccharide‐induced inflammation
Wu, Y.-T., Jin, F., Wang, Y.-L., Li, F., Wang, L., Wang, Q., Ren, Z., & Wang, Y.-F. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.11.027 · Cited by 70
“During inflammatory responses, NF-κB is phosphorylated and translocated into the nucleus, where it induces the expression of genes involved in immune and inflammatory responses (Karin and Ben-Neriah, 2000; Ben-Neriah, 2002).”
Background
Mechanism of Nicotiflorin in San-Ye-Qing rhizome for anti-inflammatory effect in ulcerative colitis.
Ruan, Y., Zhu, X.-L., Shen, J., Chen, H., & Zhou, G. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155564 · Cited by 69
A study of differential circRNA and lncRNA expressions in COVID-19-infected peripheral blood
Wu, Y., Zhao, T., Deng, R., Xia, X., Li, B., & Wang, X. (2021) · Scientific Reports · doi:10.1038/s41598-021-86134-0 · Cited by 67
A novel polysaccharide from Acorus tatarinowii protects against LPS-induced neuroinflammation and neurotoxicity by inhibiting TLR4-mediated MyD88/NF-κB and PI3K/Akt signaling pathways
Zhong, J., Qiu, X., Yu, Q., Chen, H., & Yan, C. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.06.266 · Cited by 80
Cortisol modulates inflammatory responses in LPS-stimulated RAW264.7 cells via the NF-κB and MAPK pathways
Dong, J.-S., Li, J.-J., Cui, L.-Y., Wang, Y., Lin, J.-Q., Qu, Y., & Wang, H. (2018) · BMC Veterinary Research · doi:10.1186/s12917-018-1360-0 · Cited by 69
Alantolactone, a natural sesquiterpene lactone, has potent antitumor activity against glioblastoma by targeting IKKβ kinase activity and interrupting NF-κB/COX-2-mediated signaling cascades
Wang, X., Yu, Z., Wang, C., Cheng, W., Tian, X., Huo, X., Wang, Y., Sun, C., Feng, L., Xing, J., et al. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0563-8 · Cited by 72
“these dimers to translocate to the nucleus and promote gene transcription [27].”
An evaluation of the effects of probiotics on tumoral necrosis factor (TNF-α) signaling and gene expression
Vincenzi, A., Goettert, M. I., & de Souza, C. F. V. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.10.004 · Cited by 80
Osthole inhibited TGFβ-induced epithelial–mesenchymal transition (EMT) by suppressing NF-κB mediated Snail activation in lung cancer A549 cells
Feng, H., Lu, J., Wang, Y., Pei, L., & Chen, X. (2017) · Cell Adhesion & Migration · doi:10.1080/19336918.2016.1259058 · Cited by 65
“Activation of NF-kB involves the phosphorylation, ubiquitination, and degradation of IkBa and the phosphorylation of p65, which leads to translocation of NF-kB p65 to the nucleus, where it binds to specific response elements in the DNA.(39) The increased phosphorylation of IkBa suggested that TGF-b1 promote p65 transl…”
Background
The COP9 Signalosome: A Multi-DUB Complex
Dubiel, W., Chaithongyot, S., Dubiel, D., & Naumann, M. (2020) · Biomolecules · doi:10.3390/biom10071082 · Cited by 67
Beta-sitosterol and its derivatives repress lipopolysaccharide/d-galactosamine-induced acute hepatic injury by inhibiting the oxidation and inflammation in mice.
Yin, Y., Liu, X., Liu, J., Cai, E.-B., Zhu, H.-Y., Li, H.-J., Zhang, L.-X., Li, P.-Y., & Zhao, Y. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.03.073 · Cited by 67
O-GlcNAcylation in immunity and inflammation: An intricate system (Review)
Yu, L. S., Xie, M.-Z., Men, L., & Du, J. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4238 · Cited by 75
“Through its acidic transactivation domain, p65 has the capacity to interact with several different transcriptional regulatory proteins, such as CREB‐binding protein (CBP)/p300, to initiate transcription of NF‐κB target genes (44,45).”
Background
MKL1 defines the H3K4Me3 landscape for NF-κB dependent inflammatory response
Yu, L., Fang, F., Dai, X. J., Xu, H., Qi, X., Fang, M., & Xu, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-00301-w · Cited by 71
The role of the Hippo pathway in the pathogenesis of inflammatory bowel disease
Xie, Z., Wang, Y., Yang, G., Han, J., Zhu, L., Li, L., & Zhang, S. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03395-3 · Cited by 78
Overview of Research Development on the Role of NF-κB Signaling in Mastitis
Khan, M. Z., Khan, A. A., Xiao, J., Ma, J., Ma, Y., Chen, T., Shao, D., & Cao, Z. (2020) · Animals · doi:10.3390/ani10091625 · Cited by 69
NFκB promotes oxidative stress-induced necrosis and ischemia/reperfusion injury by inhibiting Nrf2-ARE pathway
Guo, X., Hong, S., He, H., Zeng, Y., Chen, Y., Mo, X., Li, J., Li, L., Steinmetz, R. N., & Liu, Q. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.031 · Cited by 72
Renoprotection of dapagliflozin in human renal proximal tubular cells via the inhibition of the high mobility group box 1‑receptor for advanced glycation end products‑nuclear factor‑κB signaling pathway
Yao, D., Wang, S., Wang, M., & Lu, W. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9393 · Cited by 60
“NF-κ B is an important transcription factor involved in the regulation of inflammation, immune responses, cell survival and proliferation (13).”
Protective role of flavonoid baicalin from Scutellaria baicalensis in periodontal disease pathogenesis: A literature review.
Jiang, M., Li, Z.-N., & Zhu, G.-X. (2018) · Complementary Therapies in Medicine · doi:10.1016/j.ctim.2018.03.010 · Cited by 65
RNA-Sequencing for profiling goat milk transcriptome in colostrum and mature milk
Crisà, A., Ferrè, F., Chillemi, G., & Moioli, B. (2016) · BMC Veterinary Research · doi:10.1186/s12917-016-0881-7 · Cited by 65
Ketone Bodies Attenuate Wasting in Models of Atrophy
Koutnik, A., Poff, A., Ward, N. P., Deblasi, J., Soliven, M. A., Romero, M., Roberson, P. A., Fox, C. D., Roberts, M., & D'Agostino, D. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12554 · Cited by 64
“TNF-α has also been shown to play a direct role in skeletal muscle atrophy by upregulating NF-κB and subsequently ubiquitin proteasome activity.(59,60) Following prior confirmation of TNF-α elevation (Figure 3D), NF-κB activation was explored in VM-M3 skeletal muscle to determine which upstream pathway was associated…”
Antimalarial drug mefloquine inhibits nuclear factor kappa B signaling and induces apoptosis in colorectal cancer cells
Xu, X., Wang, J., Han, K.-K., Li, S.-Y., Xu, F., & Yang, Y. (2018) · Cancer Science · doi:10.1111/cas.13540 · Cited by 63
“To understand the mechanisms of inhibiting p65 phosphorylation and NF-jB transactivation by mefloquine, we examined the statuses of upstream regulatory molecules IjBa, IKKa and IKKb in RKO and HCT116 cells.(21) As shown in Figure 3A, exposure to mefloquine for 15 minutes resulted in a significant decrease of phosphory…”
Method
Macrophage migration inhibitory factor interacts with thioredoxin-interacting protein and induces NF-κB activity.
Kim, M. J., Kim, W., Kim, D., Byun, J.-E., Huy, H., Lee, S.-Y., Song, H., Park, Y.-J., Kim, T.-D., Yoon, S., et al. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.03.007 · Cited by 63
“tumor-necrosis factor (TNF) and hormones [3,4].”
Inflammation-Induced Expression and Secretion of MicroRNA 122 Leads to Reduced Blood Levels of Kidney-Derived Erythropoietin and Anemia.
Rivkin, M., Simerzin, A., Zorde-Khvalevsky, E., Chai, C., Yuval, J., Rosenberg, N., Harari-Steinfeld, R., Schneider, R., Amir, G., Condiotti, R., et al. (2016) · Gastroenterology · doi:10.1053/j.gastro.2016.07.031 · Cited by 62
Bifurcation of signalling in human innate immune pathways to NF-kB and IRF family activation
Kusiak, A., & Brady, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115246 · Cited by 68
Proinflammatory Cytokines and Skin Wound Healing in Mice
Nosenko, M. A., Ambaryan, S. G., & Drutskaya, M. S. (2019) · Molecular Biology · doi:10.1134/s0026893319050121 · Cited by 110
Dopamine activates NF-κB and primes the NLRP3 inflammasome in primary human macrophages
Nolan, R. A., Reeb, K. L., Rong, Y., Matt, S. M., Johnson, H. S., Runner, K., & Gaskill, P. J. (2019) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2019.100030 · Cited by 54
“Degradation of IκB releases the NF-κB p65 subunit, enabling the phosphorylation of this protein (Karin and Ben-Neriah, 2000).”
Ubiquitin proteasome system in immune regulation and therapeutics
Bhat, S. A., Vasi, Z., Adhikari, R., Gudur, A., Ali, A., Jiang, L., Ferguson, R., Liang, D., & Kuchay, S. (2022) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2022.102310 · Cited by 69
Elevated expression of the rhythm gene NFIL3 promotes the progression of TNBC by activating NF-κB signaling through suppression of NFKBIA transcription
Yang, W.-W., Li, J., Zhang, M.-H., Yu, H.-R., Zhuang, Y., Zhao, L., Ren, L.-L., Gong, J., Bi, H.-L., Zeng, L., et al. (2021) · Journal of experimental & clinical cancer research : CR · doi:10.1186/s13046-022-02260-1 · Cited by 59
Curdlan oligosaccharides having higher immunostimulatory activity than curdlan in mice treated with cyclophosphamide.
Tang, J., Zhen, H.-M., Wang, N.-N., Yan, Q., Jing, H., & Jiang, Z.-Q. (2019) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.10.120 · Cited by 59
Nicotine stimulates IL-8 expression via ROS/NF-κB and ROS/MAPK/AP-1 axis in human gastric cancer cells
Lian, S., Li, S., Zhu, J., Xia, Y., & Jung, Y. D. (2021) · Toxicology · doi:10.1016/j.tox.2021.153062 · Cited by 65
Inhibitory effect on HT-29 colon cancer cells of a water-soluble polysaccharide obtained from highland barley
Cheng, D., Zhang, X., Meng, M., Han, L., Li, C., Hou, L., Qi, W., & Wang, C. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.06.099 · Cited by 63
Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates
Li, C.-Q., Moro, S., Shostak, K., O'Reilly, F. J., Donzeau, M., Graziadei, A., McEwen, A., Desplancq, D., Poussin-Courmontagne, P., Bachelart, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52076-0 · Cited by 57
Nrf2/HO-1 as a therapeutic target in renal fibrosis
Hassanein, E. H. M., Ibrahim, I. M., Abd‐alhameed, E. K., Sharawi, Z. W., Jaber, F. A., & Althagafy, H. S. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122209 · Cited by 58
NF-κB signaling regulates the formation of proliferating Müller glia-derived progenitor cells in the avian retina
Palazzo, I., Deistler, K. A., Hoang, T. V., Blackshaw, S., & Fischer, A. (2019) · Development · doi:10.1101/724260 · Cited by 57
“degradation, thereby resulting in liberation of NF-κB transcription factors (Karin and Ben-Neriah, 2000; Zhang et al., 2017).”
Background
Targeting HMGB1 TLR4 signaling as a novel approach to treatment of cerebral ischemia
Yang, Q.-W. (2010) · Frontiers in Bioscience · doi:10.2741/s119 · Cited by 55
Interleukin-1β and TNF-α systems in ovarian follicles and their roles during follicular development, oocyte maturation and ovulation
Silva, J., Lima, F. E. O., Souza, A., & Silva, A. (2020) · Zygote (Cambridge. Print) · doi:10.1017/s0967199420000222 · Cited by 56
“…NF-κB pathway occurs with the phosphorylation of two serine residues (ser32 and ser36) of the IκB protein by IκB kinase activity (IKK), the polyubiquitination of IKKβ and then degradation by the 26S proteosome, releasing NF-κB dimers (p65 and p50) (Nishikori, 2005; Karin and Ben-Neriah, 2000).”
Background
Activation of NF-κB in B cell receptor signaling through Bruton’s tyrosine kinase-dependent phosphorylation of IκB-α
Pontoriero, M., Fiume, G., Vecchio, E., de Laurentiis, A., Albano, F., Iaccino, E., Mimmi, S., Pisano, A., Agosti, V., Giovannone, E. D., et al. (2019) · Journal of Molecular Medicine · doi:10.1007/s00109-019-01777-x · Cited by 58
Cardioprotective Effects of Malvidin Against Isoproterenol-Induced Myocardial Infarction in Rats: A Mechanistic Study
Wei, H., Li, H., Wan, S., Zeng, Q., Cheng, L.-X., Jiang, L.-L., & Peng, Y.-D. (2017) · Medical Science Monitor · doi:10.12659/msm.902196 · Cited by 56
“Additionally, the results also demonstrated that nuclear translocation of Nrf-2 and subsequent HO-1 expression might be associated with nuclear factor kappa B (NF-kB) pathway activation.”
BackgroundInfluential
p38-mediated FOXN3 phosphorylation modulates lung inflammation and injury through the NF-κB signaling pathway
Zhu, X., Huang, B., Zhao, F., Lian, J., He, L., Zhang, Y., Ji, L., Zhang, J., Yan, X., Zeng, T., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad057 · Cited by 61

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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