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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“Under normal unstressed conditions, NF-κB is held in the cytoplasm by its inhibitory protein, IκB, but when ROS levels rise, IκB is phosphorylated, ubiquitinated and targeted for degradation, leaving NF-κB free to translocate into the nucleus and upregulate antioxidant genes [10].”
Background
FOXO4 ameliorates alcohol-induced chronic liver injury via inhibiting NF-κB and modulating gut microbiota in C57BL/6J mice.
Sang, L.-X., Kang, K., Sun, Y., Li, Y.-L., & Chang, B. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107572 · Cited by 26
Interleukin-36 Cytokine/Receptor Signaling: A New Target for Tissue Fibrosis
Melton, E. M., & Qiu, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186458 · Cited by 28
“kappa-light-chain-enhancer of activated B cells (NFKB) dependent upregulation of pro-inflammatory gene expression (Figure 1) [31,37].”
Background
Determinants of Sensitivity to Radiotherapy in Endometrial Cancer
Sorolla, M. A., Parisi, E., & Sorolla, A. (2020) · Cancers · doi:10.3390/cancers12071906 · Cited by 27
Peer Review #1 of "Novel association between TGFA, TGFB1, IRF1, PTGS2 and IKBKB single-nucleotide polymorphisms and occurrence, severity and treatment response of major depressive disorder (v0.1)"
Białek, K., Czarny, P., Watała, C., Wigner, P., Talarowska, M., Gałecki, P., Szemraj, J., & Śliwiński, T. (2020) · PeerJ · doi:10.7287/peerj.8676v0.1/reviews/1
A dual role for hepatocyte-intrinsic canonical NF-κB signaling in virus control
Namineni, S., O'Connor, T., Faure-Dupuy, S., Johansen, P., Riedl, T., Liu, K.-J., Xu, H.-F. C., Singh, I., Shinde, P. V., Li, F.-H., et al. (2020) · Zeitschrift für Gastroenterologie - German Journal of Gastroenterology · doi:10.1055/s-0039-3402260 · Cited by 26
“The IKK complex consists of two catalytic 11 kinase subunits, IKKα and IKKβ with intrinsic kinase activities and a regulatory 12 subunit, IKKγ, also known as NF-κB essential modulator (NEMO) with helix-loop 13 helix and leucine-zipper motifs that mediate protein-protein interactions (15, 16).”
BackgroundSelf-citation
Pseudoginsenoside-F11 Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Suppressing Neutrophil Infiltration and Accelerating Neutrophil Clearance
Wang, P.-W., Hou, Y., Zhang, W., Zhang, H.-T., Che, X.-H., Gao, Y., Liu, Y., Yang, D., Wang, J.-M., Xiang, R.-W., et al. (2019) · Inflammation · doi:10.1007/s10753-019-01047-5 · Cited by 26
Alternate NF-κB-Independent Signaling Reactivation of Latent HIV-1 Provirus
Acchioni, C., Remoli, A. L., Marsili, G., Acchioni, M., Nardolillo, I., Orsatti, R., Farcomeni, S., Palermo, E., Perrotti, E., Barreca, M. L., et al. (2019) · Journal of Virology · doi:10.1128/jvi.00495-19 · Cited by 26
“Five members of the family, C-Rel, RelA (p65), RelB, NF- B1 (p50 and its precursor, p105), and NF- B2 (p52 and its precursor, p100), exist as homodimers or heterodimers in quiescent or unstimulated cells, in association with the inhibitory inhibitor of nuclear factor B (I B), in particular, I B- , which maintains the…”
Background
Role of the COP9 Signalosome (CSN) in Cardiovascular Diseases
Milic, J., Tian, Y., & Bernhagen, J. (2019) · Biomolecules · doi:10.3390/biom9060217 · Cited by 27
“In the context of this review article, substrate receptor F-box protein/‘to-be-degraded-substrate’ pairs related to cell cycle progression, inflammatory signaling, or hypoxic stress such as SCFβ-TRCP1/IκB-α, SCFβ-TRCP1/Wee1, SCFβ-TRCP1/Cdc25A, Cul3KEAP1/Nrf2, SCFSkp2/p27, or Cul2VHL/HIF-1α, respectively, are of partic…”
BackgroundInfluential
Morin Alleviates Vincristine-Induced Neuropathic Pain via Nerve protective Effect and Inhibition of NF-κB Pathway in Rats
Jiang, K., Shi, J., & Shi, J. (2019) · Cellular and molecular neurobiology · doi:10.1007/s10571-019-00679-3 · Cited by 26
Suppressive effects of the supercritical-carbon dioxide fluid extract of Chrysanthemum indicum on chronic unpredictable mild stress-induced depressive-like behavior in mice
Wu, X., Tang, B.-Q., Liao, X., Su, Z., Lee, S. M., Cai, Y., & Li, C. (2019) · Food & Function · doi:10.1039/c8fo02474j · Cited by 29
A20 Orchestrates Inflammatory Response in the Oral Mucosa through Restraining NF-κB Activity
Li, Y., Mooney, E. C., Holden, S. E., Xia, X., Cohen, D. J., Walsh, S. W., Ma, A. I., & Sahingur, S. E. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801286 · Cited by 27
Isoalantolactone inhibits IKKβ kinase activity to interrupt the NF‐κB/COX‐2‐mediated signaling cascade and induces apoptosis regulated by the mitochondrial translocation of cofilin in glioblastoma
Xing, J., Wang, X., Lan, Y., Lou, J., Ma, B., Zhu, T., Zhang, H., Wang, D., Yu, Z., Yuan, Z., et al. (2019) · Cancer Medicine · doi:10.1002/cam4.2013 · Cited by 27
Human NF-κB1 Haploinsufficiency and Epstein–Barr Virus-Induced Disease—Molecular Mechanisms and Consequences
Hoeger, B., Serwas, N. K., & Boztuǧ, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01978 · Cited by 30
Targeting Oncogenic Nuclear Factor Kappa B Signaling with Redox-Active Agents for Cancer Treatment
Fouani, L., Kovačević, Ž., & Richardson, D. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7387 · Cited by 26
“…of the catalytic portion of the I jja / b component activates this complex, which may then use its inherent kinase activity to double phosphorylate the I j B a inhibitory protein on its substrate recognition sites (serine-32 and serine-36 for I j B a ) (125, 157, 225, 320, 340, 356, 370).”
Mumps Virus SH Protein Inhibits NF-κB Activation by Interacting with Tumor Necrosis Factor Receptor 1, Interleukin-1 Receptor 1, and Toll-Like Receptor 3 Complexes
Franz, S., Rennert, P., Woznik, M., Grützke, J., Lüdde, A., País, E. M. A., Finsterbusch, T., Geyer, H., Mankertz, A., & Friedrich, N. (2017) · Journal of Virology · doi:10.1128/jvi.01037-17 · Cited by 26
“Consequently, p65 is transported into the nucleus and binds to its specific target DNA sequences (28).”
Background
TREM2-mediated regulation of myeloid cells in the tumor microenvironment: new insights and therapeutic prospects
Huang, Y., & Fang, W. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01152-9 · Cited by 30
Sphingosine 1-phosphate receptor 2 mediated early stages of pancreatic and systemic inflammatory responses via NF-kappa B activation in acute pancreatitis
Yang, J., Tang, X., Li, B.-Q., & Shi, J. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00971-8 · Cited by 25
“Then, NF-κB translocates to the nucleus; and binds to specific elements located in the promoters of various genes, such as inflammatory factors, and adhesion molecules [13, 14].”
Background
Paclitaxel resistance is mediated by NF‑κB on mesenchymal primary breast cancer cells
Esparza‐López, J., Longoria, O., la Cruz-Escobar, E. N. D., Garibay-Díaz, J. C., León‐Rodríguez, E., & Ibarra-Sánchez, M. D. J. (2021) · Oncology Letters · doi:10.3892/ol.2021.13168 · Cited by 25
“Next, NF‐κB is translocated to the nucleus where it regulates the expression of its target genes (19).”
Therapeutic perspective of thiosemicarbazones derivatives in inflammatory pathologies: A summary of in vitro/in vivo studies
Kanso, F., Khalil, A., Noureddine, H., & El-Makhour, Y. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107778 · Cited by 40
Targeting Inflammatory Mediators: An Anticancer Mechanism of Thymoquinone Action
Akter, Z., Ahmed, F. H., Tania, M., & Khan, M. A. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666191011143642 · Cited by 33
Провоспалительные цитокины и заживление кожных ран у мышей
Nosenko, M. A., Амбарян, С. Г., & Друцкая, М. С. (2019) · Molecular Biology · doi:10.1134/s0026898419050136 · Cited by 46
DNA damage-induced activation of ATM promotes β-TRCP-mediated ARID1A ubiquitination and destruction in gastric cancer cells
Jiang, Z., Peng, T., Qian, H.-L., Lu, C., Qiu, F., & Zhang, S.-Z. (2019) · Cancer Cell International · doi:10.1186/s12935-019-0878-y · Cited by 25
G‐ CSF and cognitive dysfunction in elderly diabetic mice with cerebral small vessel disease: Preventive intervention effects and underlying mechanisms
Guan, Z., Tao, Y., Zhang, X., Guo, Q., Liu, Y., Zhang, Y., Wang, Y., Ji, G., Wu, G., Wang, N., et al. (2017) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12691 · Cited by 30
Signals for Muscular Protein Turnover and Insulin Resistance in Critically Ill Patients: A Narrative Review
Chapela, S. P., Simancas‐Racines, D., Montalván, M., Frías-Toral, E., Simancas-Racines, A., Muscogiuri, G., Barrea, L., Sarno, G., Martinez, P. I., Reberendo, M. J., et al. (2023) · Nutrients · doi:10.3390/nu15051071 · Cited by 28
Aloe Extracts Inhibit Skin Inflammatory Responses by Regulating NF-κB, ERK, and JNK Signaling Pathways in an LPS-Induced RAW264.7 Macrophages Model
Wang, F., Liu, J.-T., An, Q., Wang, Y., Yang, Y., Huo, T., Yang, S.-Q., Ju, R.-J., & Quan, Q. (2023) · Clinical, Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s391741 · Cited by 24
From the Evasion of Degradation to Ubiquitin-Dependent Protein Stabilization
Ahmad, Y. A., Oknin-Vaisman, A., Bitman-Lotan, E., & Orian, A. (2021) · Cells · doi:10.3390/cells10092374 · Cited by 26
“For example, upon immune challenge, signal-induced phosphorylation of the inhibitory protein, IκBα, converts the extremely stable protein into a rapidly degraded phospho-protein, enabling immune response [8,9].”
Background
A Review: Mechanism of Phyllanthus urinaria in Cancers—NF-κB, P13K/AKT, and MAPKs Signaling Activation
Saahene, R. O., Agbo, E., Barnes, P., Yahaya, E. S., Amoani, B., Nuvor, S. V., & Okyere, P. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/4514342 · Cited by 27
Immunoproteasome Function in Normal and Malignant Hematopoiesis
Santamaría, N. T., Ebstein, F., Heidel, F. H., & Krüger, E. (2021) · Cells · doi:10.3390/cells10071577 · Cited by 25
Protective Effects of SPA0355, a Thiourea Analogue, Against Lipopolysaccharide-Induced Acute Kidney Injury in Mice
Kim, J.-Y., Leem, J., & Hong, H.-L. (2020) · Antioxidants · doi:10.3390/antiox9070585 · Cited by 24
“Phosphorylated IkB is subsequently ubiquitinated and degraded by the proteasomal pathway, thus allowing NF-kB to translocate into the nucleus, where it modulates the expression of inflammatory target genes [24].”
Background
Inhibition of microRNA-128-3p alleviates liver ischaemia–reperfusion injury in mice through repressing the Rnd3/NF‐ κ B axis
Mou, T., Luo, Y., Huang, Z., Zheng, D., Pu, X., Shen, A., Pu, J., Li, T., Dai, J., Chen, W., et al. (2020) · Innate Immunity · doi:10.1177/1753425920928449 · Cited by 25
Anti-Inflammatory and Protein Tyrosine Phosphatase 1B Inhibitory Metabolites from the Antarctic Marine-Derived Fungal Strain Penicillium glabrum SF-7123
Tran, H. M., Kim, D.-C., Sohn, J., Yim, J., & Oh, H. (2020) · Marine Drugs · doi:10.3390/md18050247 · Cited by 24
PCAT‐1 promotes cell growth by sponging miR‐129 via MAP3K7/NF‐κB pathway in multiple myeloma
Shen, X., Kong, S., Yang, Q., Yin, Q., Cong, H., Wang, X., & Ju, S. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15035 · Cited by 26
Telmisartan, an angiotensin II receptor blocker, attenuates Prevotella intermedia lipopolysaccharide-induced production of nitric oxide and interleukin-1β in murine macrophages
Choe, S.-H., Choi, E., Hyeon, J.-Y., Keum, B. R., Choi, I. S., & Kim, S. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.105750 · Cited by 24
Glucocorticoids delay RAF-induced senescence promoted by EGR1
Carvalho, C., L’Hôte, V., Courbeyrette, R., Kratassiouk, G., Pinna, G., Cintrat, J., Wilkes, C. D., Derbois, C., Olaso, R., Deleuze, J., et al. (2019) · Journal of Cell Science · doi:10.1242/jcs.230748 · Cited by 27
“…in RAF-induced proliferative arrest by constructing a version of our BJhTert/ptetON-B-RAF-V600E cell line that expresses the IκB-SR (super repressor), a mutant version of IκB that acts as a dominant-negative suppressor of NF-κB by sequestering RelA in the cytoplasm (Karin and Ben-Neriah, 2000).”
Background
Combined inhibition of Bcl-2 and NFκB synergistically induces cell death and limits xenograft mouse tumor growth in CTCL.
Froehlich, T. C., Müller-Decker, K., Braun, J., Albrecht, T., Schroeder, A. E., Gülow, K., Goerdt, S., Krammer, P., & Nicolay, J. (2019) · Blood · doi:10.1182/blood.2019001545 · Cited by 24
TRAF2 Cooperates with Focal Adhesion Signaling to Regulate Cancer Cell Susceptibility to Anoikis
da Silva, S. D., Xu, B., Maschietto, M. C., Marchi, F. A., Alkailani, M. I., Bijian, K., Xiao, D., & Alaoui‐Jamali, M. A. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-1261 · Cited by 28
“Activated IKKs thus phosphorylate IkBs at serine residues 32 and 36, leading to their degradation and the subsequent activation of NF-kB (23, 26).”
Background
Activation of the porcine alveolar macrophages via toll-like receptor 4/NF-κB mediated pathway provides a mechanism of resistin leading to inflammation
Li, B., Fang, J. S., Zuo, Z., Yin, S., He, T., Yang, M., Deng, J., Shen, L., Ma, X., Yu, S., et al. (2018) · Cytokine · doi:10.1016/j.cyto.2018.04.002 · Cited by 23
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-кB activation
Wu, Z., Neufeld, H. L. D., Torlakovic, E., & Xiao, W. (2018) · OncoTarget · doi:10.18632/oncotarget.24640 · Cited by 24
Infection with Classical Swine Fever Virus Induces Expression of Type III Interferons and Activates Innate Immune Signaling
Cai, B.-X., Bai, Q.-L., Chi, X., Goraya, M. U., Wang, L., Wang, S.-L., Chen, B., & Chen, J.-L. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02558 · Cited by 24
A novel statistical approach for identification of the master regulator transcription factor
Sikdar, S., & Datta, S. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1499-x · Cited by 24
Huangqi Baihe Granules alleviate hypobaric hypoxia-induced acute lung injury in rats by suppressing oxidative stress and the TLR4/NF-κB/NLRP3 inflammatory pathway.
Zeng, Y.-D., Cao, W., Huang, Y., Zhang, H., Li, C., He, J.-Z., Liu, Y.-Q., Gong, H.-X., & Su, Y. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117765 · Cited by 23
Translational fidelity screens in mammalian cells reveal eIF3 and eIF4G2 as regulators of start codon selectivity
She, R., Luo, J., & Weissman, J. S. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad329 · Cited by 28
Small molecules of herbal origin for osteoarthritis treatment: in vitro and in vivo evidence
Zhang, P., Li, K., Kamali, A., Ziadlou, R., Ahmad, P., Wang, X.-L., Richards, R., Alini, M., Basoli, V., Li, Z., et al. (2022) · Arthritis Research & Therapy · doi:10.1186/s13075-022-02785-y · Cited by 23
Natural Products as Novel Neuroprotective Agents; Computational Predictions of the Molecular Targets, ADME Properties, and Safety Profile
Alghamdi, S. S., Suliman, R. S., Aljammaz, N. A., Kahtani, K. M., Aljatli, D., & Albadrani, G. M. (2022) · Plants · doi:10.3390/plants11040549 · Cited by 29
“The activation of NF-κB results in the phosphorylation of NF-κB inhibitor, IκB, via the IκB kinase (IKK) signalosome complex leading to transcription of pro-inflammatory mediators, such as iNOS, COX-2, TNF-α, and IL-1β [80,81] Therefore, inhibiting the NF-κB will suppress the release of these inflammatory markers, whi…”
Background
Discovery of Phenolic Glycoside from Hyssopus cuspidatus Attenuates LPS-Induced Inflammatory Responses by Inhibition of iNOS and COX-2 Expression through Suppression of NF-κB Activation
Liu, X., Su, J., Wang, G., Zheng, L.-H., Wang, G.-N., Sun, Y., Bao, Y.-L., Wang, S., & Huang, Y.-X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212128 · Cited by 23
Two methoxy derivatives of resveratrol, 3,3′,4,5′-tetramethoxy-trans-stilbene and 3,4′,5-trimethoxy-trans-stilbene, suppress lipopolysaccharide-induced inflammation through inactivation of MAPK and NF-κB pathways in RAW 264.7 cells
Zhou, C., Zhang, X., Ruan, C., & Cheang, W. S. (2021) · Chinese Medicine · doi:10.1186/s13020-021-00480-9 · Cited by 25
Discovery of RSV-Induced BRD4 Protein Interactions Using Native Immunoprecipitation and Parallel Accumulation—Serial Fragmentation (PASEF) Mass Spectrometry
Mann, M. W., Roberts, D. S., Zhu, Y., Li, Y., Zhou, J., Ge, Y., & Brasier, A. R. (2021) · Viruses · doi:10.3390/v13030454 · Cited by 23
“BRD4-dependent transcriptional elongation involves the coordinated actions 47 of histone acetyl transferases [15,16], cyclin dependent kinases [8] and ubiquitin ligases 48 [17] that dissociate elongation factors and stimulate polymerase processivity.”
Background
Sophorasubprosrate polysaccharide suppress the inflammatory reaction of RAW264.7 cells infected with PCV2 via regulation NF-κB/MAPKs/c-Jun signal pathway and histone acetylation modification.
Yang, J., Cao, M., Hu, W.-Y., Wei, Y.-Y., & Hu, T.-J. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.128 · Cited by 23
A20 Restricts Inflammatory Response and Desensitizes Gingival Keratinocytes to Apoptosis
Li, Y., Mooney, E. C., Xia, X., Gupta, N., & Sahingur, S. E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00365 · Cited by 24
Thrombin Induces Secretion of Multiple Cytokines and Expression of Protease-Activated Receptors in Mouse Mast Cell Line
Fang, X., Liao, R., Yu, Y., Li, J., Guo, Z., & Zhu, T. (2019) · Mediators of Inflammation · doi:10.1155/2019/4952131 · Cited by 27
“It was well known that NF-κB and MAPK cell signaling pathways play an important role in the process of inflammation and immunity [17, 33].”
Background
Dauricine negatively regulates lipopolysaccharide- or cecal ligation and puncture-induced inflammatory response via NF-κB inactivation.
Qiao, B., Wang, H., Wang, C., Liang, M.-L., Huang, K., & Li, Y.-Q. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.03.018 · Cited by 23
Improving hyperglycemic effect of FGF‐21 is associated with alleviating inflammatory state in diabetes
Wang, N., Xu, T.-Y., Zhang, X., Li, J.-Y., Wang, Y.-X., Guo, X.-C., Li, S.-M., Wang, W.-F., & Li, D.-S. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.01.048 · Cited by 23
The Calcium-Induced Regulation in the Molecular and Transcriptional Circuitry of Human Inflammatory Response and Autoimmunity
Dias, I. R. D. S. R., Mok, S., Gordillo-Martínez, F., Khan, I., Hsiao, W. L., Law, B., Wong, V., & Liu, L. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00962 · Cited by 23
“…2014; Storr et al., 2011, 2015) (green boxes and arrows; includes NFKB1, which encodes the precursor protein of p50, one of the subunits of NF-κB, Karin and Ben-Neriah, 2000), JAK/STAT axis (purple boxes and arrows; includes STAT3) (Pothlichet et al., 2008; Miyazaki et al., 2015), and the…”
BackgroundInfluential
Mycobacterium indicus pranii (Mw) inhibits invasion by reducing matrix metalloproteinase (MMP-9) via AKT/ERK-1/2 and PKCα signaling: A potential candidate in melanoma cancer therapy
Halder, K., Banerjee, S., Ghosh, S., Bose, A., Das, S., Chowdhury, B., & Majumdar, S. (2017) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1078024 · Cited by 23
“The released NF-kB translocates into the nucleus and binds to the promoter region of MMP-9, leading to gene expression.(45) On the other hand, AP-1 is a nuclear transcription factor comprising homodimers and heterodimers of members of the Fos and Jun families.”
Background
Humanin inhibits apoptosis in pituitary tumor cells through several signaling pathways including NF-κB activation
Gottardo, M. F., Ayala, M. M., Ferraris, J., Zárate, S., Pisera, D. A., Candolfi, M., Jaita, G., & Seilicovich, A. (2017) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-017-0388-4 · Cited by 23
Homocysteine regulates endothelin type B receptors in vascular smooth muscle cells.
Chen, Y., Zhang, H.-M., Liu, E.-Q., Xu, C.-B., & Zhang, Y.-P. (2016) · Vascular pharmacology · doi:10.1016/j.vph.2016.08.011 · Cited by 23
NFKB1 as a key player in Tumor biology: from mechanisms to therapeutic implications
Song, Z., Feng, Z., Wang, X., Li, J., & Zhang, D. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-024-09974-2 · Cited by 22
Overview of pyroptosis mechanism and in-depth analysis of cardiomyocyte pyroptosis mediated by NF-κB pathway in heart failure
Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117367 · Cited by 22
The role of NF-κB-SOX9 signalling pathway in osteoarthritis
Tian, B., Zhang, L., Zheng, J., & Kang, X. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e37191 · Cited by 27
“Only after I κ B is phosphorylated and degraded by proteasome can NF-κ B dimer be released into the nucleus for transcriptional activation to regulate the expression of inflammatory factors [21,22].”
Background
Himalayan Wild Fruits as a Strong Source of Nutraceuticals, Therapeutics, Food and Nutrition Security
Semwal, P., Painuli, S., Jamloki, A., Rauf, A., Rahman, M., Olatunde, A., Hemeg, H., Abu-Izneid, T., Naz, S., Bangar, S. P., et al. (2022) · Food reviews international (Print) · doi:10.1080/87559129.2022.2121407 · Cited by 22
Aryl Hydrocarbon Receptor (AhR) Limits the Inflammatory Responses in Human Lung Adenocarcinoma A549 Cells via Interference with NF-κB Signaling
Vázquez-Gómez, G., Karasová, M., Tylichová, Z., Kabátková, M., Hampl, A., Matthews, J. B., Neča, J., Cigánek, M., Machala, M., & Vondráček, J. (2022) · Cells · doi:10.3390/cells11040707 · Cited by 24
Zearalenone induces immuno-compromised status via TOR/NF/κB pathway and aggravates the spread of Aeromonas hydrophila to grass carp gut (Ctenopharyngodon idella)
Zhang, H., Wang, Y., Zhou, X., Jiang, W., Wu, P., Liu, Y., Zhang, L., Mi, H., Jiang, J., Kuang, S., et al. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.112786 · Cited by 26
Differential impacts of brain stem oxidative stress and nitrosative stress on sympathetic vasomotor tone
Chan, J. Y. H., & Chan, S. H. H. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.05.015 · Cited by 25
Interaction of PIAS1 with PRRS virus nucleocapsid protein mediates NF-κB activation and triggers proinflammatory mediators during viral infection
Ke, H.-Z., Lee, S., Kim, J., Liu, H.-C. S., & Yoo, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-47495-9 · Cited by 22
COP9 Signalosome Interaction with UspA/Usp15 Deubiquitinase Controls VeA-Mediated Fungal Multicellular Development
Meister, C., Thieme, K. G., Thieme, S., Köhler, A. M., Schmitt, K., Valerius, O., & Braus, G. (2019) · Biomolecules · doi:10.3390/biom9060238 · Cited by 22
“β-TrCP targets the physically interacting inhibitor of NF-κB for ubiquitination and subsequent degradation [38,91,92].”
Comparison of the Hepatoprotective Effects of the Three Main Stilbenes from Mulberry Twigs.
Jia, Y.-N., Peng, Y.-L., Zhao, Y., Cheng, X., Zhou, Y., Chai, C., Zeng, L., Pan, M., & Xu, L. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b07245 · Cited by 22
Inhibitory Effect of Ficin Derived from Fig Latex on Inflammation and Melanin Production in Skin Cells
Cho, U., Choi, D.-H., Yoo, D., Park, S., & Hwang, H. (2019) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-019-0010-0 · Cited by 22
Negative regulation of the RLH signaling by the E3 ubiquitin ligase RNF114
Lin, B., Qi, K., Li, H., Pheifer, N. S., Velliquette, D., & Leaman, D. W. (2017) · Cytokine · doi:10.1016/j.cyto.2017.05.002 · Cited by 23
“In addition, TRAF2 and TRAF6 activated by MAVS induce IKKα/ IKKβ/NF-κB essential modulator (NEMO) complex to transcriptionally regulate IFNs and inflammatory genes via NF-κB [10,11].”
BackgroundInfluential
Enhanced migration of murine fibroblast-like 3T3-L1 preadipocytes on type I collagen-coated dish is reversed by silibinin treatment
Liu, X.-L., Xu, Q., Liu, W.-W., Yao, G.-D., Zhao, Y.-L., Xu, F., Hayashi, T., Fujisaki, H., Hattori, S., Tashiro, S.-I., et al. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3173-z · Cited by 22
Development and Characterisation of a Novel NF-κB Reporter Cell Line for Investigation of Neuroinflammation
Zeuner, M.-T., Vallance, T., Vaiyapuri, S., Cottrell, G., & Widera, D. (2017) · Mediators of Inflammation · doi:10.1155/2017/6209865 · Cited by 22
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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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