Cited by 6,080Cytokine Signaling Pathways and Interactionsinterferon and immune responsesNF-κB Signaling Pathways

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

Darnell, James E., Kerr, lan M., Stark, George R.·1994·Science

DOI 10.1126/science.8197455

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Abstract

Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.

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Frequent Loss of IRF2 in Cancers Leads to Immune Evasion through Decreased MHC Class I Antigen Presentation and Increased PD-L1 Expression
Kriegsman, B. A., Vangala, P., Chen, B. J., Meraner, P., Brass, A. L., Garber, M., & Rock, K. L. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900475 · Cited by 114
Reactive Oxygen Species as Intracellular Signaling Molecules in the Cardiovascular System
Krylatov, A. V., Маслов, Л. Н., Воронков, Н. С., Boshchenko, A. A., Popov, S. V., Gomez, L., Wang, H., Jaggi, A. S., & Downey, J. M. (2018) · Current Cardiology Reviews · doi:10.2174/1573403x14666180702152436 · Cited by 144
“The family of highly conserved signal transducer and activator of transcription (STAT) include STAT1-4, 5A, 5B and 6 [128, 129].”
Background
Identification of a natural product-like STAT3 dimerization inhibitor by structure-based virtual screening
Liu, L., Leung, K., Chan, D. S.-H., Wang, Y.-T., Ma, D., & Leung, C.-H. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.250 · Cited by 123
“COS-7 cells were stimulated with IFN-g (25 ng/ml) for activation of STAT1 for 1 h.(62) HeLa cells were stimulated with IFN-a (1000 U/ml) for activation of STAT3 and STAT1 for 1 h.”
Method
Endothelial Cell Energy Metabolism, Proliferation, and Apoptosis in Pulmonary Hypertension
Xu, W., & ERZURUM, S. C. (2010) · Comprehensive physiology · doi:10.1002/cphy.c090005 · Cited by 123
“Once phosphorylated, STAT proteins form homo- or heterodimers (STAT1: STAT2, STAT1: STAT3), enter the nucleus, bind to specific DNA elements, and direct transcription (37, 87).”
Background
Curcumin Suppresses the Induction of Indoleamine 2,3-Dioxygenase by Blocking the Janus-activated Kinase-Protein Kinase Cδ-STAT1 Signaling Pathway in Interferon-γ-stimulated Murine Dendritic Cells
Jeong, Y.-I., Kim, S. W., Jung, I. D., Lee, J. S., Chang, J. H., Lee, C.-M., Chun, S. H., Yoon, M., Kim, G. T., Ryu, S. W., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807328200 · Cited by 123
TRAIL Gene Therapy: From Preclinical Development to Clinical Application
Griffith, T. S., Stokes, B., Kucaba, T. A., Earel, J. K., VanOosten, R. L., Brincks, E. L., & Norian, L. A. (2009) · Current Gene Therapy · doi:10.2174/156652309787354612 · Cited by 88
“Necrosis is the nonphysiological or passive type of cell death usually resulting from extreme cellular trauma, generally affecting groups of cells rather than individual cells, and typically evoking inflammation [4].”
Background
Murine interferon lambdas (type III interferons) exhibit potent antiviral activity in vivo in a poxvirus infection model.
Bartlett, N., Buttigieg, K., Kotenko, S., & Smith, G. L. (2005) · Journal of General Virology · doi:10.1099/vir.0.80904-0 · Cited by 117
“Once activated, this complex translocates to the nucleus, where it binds to IFN-stimulated response elements (ISRE), regulating expression of numerous genes that are required for induction of antiviral immunity (Darnell et al., 1994).”
Background
The role of Stat3 in glioblastoma multiforme
Luwor, R. B., Stylli, S. S., & Kaye, A. H. (2013) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2013.03.006 · Cited by 127
Biomechanical Thresholds Regulate Inflammation through the NF-κB Pathway: Experiments and Modeling
Nam, J., Aguda, B. D., Rath, B., & Agarwal, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005262 · Cited by 116
“Furthermore, many simplifying assumptions of the model such as ignoring the hundreds of NFkB targets that affect NOS2 expression as well as simultaneous activation of other signaling pathways involved in the regulation of NOS2 expression likely affect the equilibrium state of NF-kB [15,16,17].”
Background
Blockage of JAK/STAT signalling attenuates renal ischaemia-reperfusion injury in rats
Yang, N., Luo, M., Li, R., Huang, Y., Zhang, R., Wu, Q., Wang, F., Li, Y., & Yu, X. (2007) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfm509 · Cited by 111
“JAK activation stimulates cell proliferation, differentiation, cell migration and apoptosis [12,14,15].”
Background
Inhibition of Interferon Signaling by the Kaposi's Sarcoma-Associated Herpesvirus Full-Length Viral Interferon Regulatory Factor 2 Protein
Fuld, S., Cunningham, C., Klucher, K. M., Davison, A. J., & Blackbourn, D. J. (2006) · Journal of Virology · doi:10.1128/jvi.80.6.3092-3097.2006 · Cited by 100
Oxidized phospholipids increase interleukin 8 (IL-8) synthesis by activation of the c-src/signal transducers and activators of transcription (STAT)3 pathway
Yeh, M., Gharavi, N. M., Choi, J., Hsieh, X., Reed, E., Mouillesseaux, K. P., Cole, A. L., Reddy, S. T., & Berliner, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312198200 · Cited by 116
Salmonella Effector SteE Converts the Mammalian Serine/Threonine Kinase GSK3 into a Tyrosine Kinase to Direct Macrophage Polarization
Panagi, I., Jennings, E., Zeng, J., Günster, R. A., Stones, C. D., Mak, H., Jin, E., Stapels, D. A. C., Subari, N. Z., Pham, T. H. M., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.11.002 · Cited by 121
Regulation of melanocyte pivotal transcription factor MITF by some other transcription factors
Wan, P., Hu, Y., & He, L. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0823-4 · Cited by 115
“It is tyrosine-phosphorylated by receptor-associated Janus kinase (JAK) and translocates as a dimer into the nucleus to activate specific genes [16].”
Background
Interferon, a growing cytokine family: 50 years of interferon research
Chelbi‐Alix, M. K., & Wietzerbin, J. (2007) · Biochimie · doi:10.1016/j.biochi.2007.05.001 · Cited by 112
Regulation of the Transcriptional Activity of the IRF7 Promoter by a Pathway Independent of Interferon Signaling
Ning, S., Huye, L. E., & Pagano, J. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404260200 · Cited by 108
Regulation of Apoptosis in Myeloid Cells by Interferon Consensus Sequence–Binding Protein
Gabriele, L., Phung, J., Fukumoto, J., Segal, D., Wang, I.-M., Giannakakou, P., Giese, N. A., Ozato, K., & Morse, H. C. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.3.411 · Cited by 114
Apoptotic Cells Induced Signaling for Immune Homeostasis in Macrophages and Dendritic Cells
Trahtemberg, U., & Mevorach, D. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01356 · Cited by 125
“Stimulation of the IFNγ receptor triggers JAK-mediated tyrosine phosphorylation and subsequent dimerization of STAT1, which binds as a homodimer to elements known as gamma-activated sequences in the promoters of the genes encoding NOS2, the MHC class II transactivator, and IL-12, among others (132).”
Background
Cellular and molecular perspectives in rheumatoid arthritis
Veale, D. J., Orr, C. K., & Fearon, U. (2017) · Seminars in Immunopathology · doi:10.1007/s00281-017-0633-1 · Cited by 120
Kinome-wide RNAi studies in human multiple myeloma identify vulnerable kinase targets, including a lymphoid-restricted kinase, GRK6
Tiedemann, R. E., Zhu, Y. X., Schmidt, J. E., Yin, H. H., Shi, C.-X., Que, Q. Q., Basu, G. D., Azorsa, D. O., Perkins, L. M., Braggio, E., et al. (2009) · Blood · doi:10.1182/blood-2009-09-243980 · Cited by 106
Nipah Virus Sequesters Inactive STAT1 in the Nucleus via a P Gene-Encoded Mechanism
Ciancanelli, M. J., Volchkova, V. A., Shaw, M. L., Volchkov, V. E., & Basler, C. F. (2009) · Journal of Virology · doi:10.1128/jvi.02610-08 · Cited by 129
“STAT protein activation involves tyrosine phosphorylation by JAK family kinases, resulting in STAT homo- or heterodimerization via SH2 domainphosphotyrosine interactions (10, 28, 35).”
Background
Immune evasion by pathogens of bovine respiratory disease complex
Srikumaran, S., Kelling, C., & Ambagala, A. (2007) · Animal Health Research Reviews · doi:10.1017/s1466252307001326 · Cited by 114
“IFNs induce an anti-viral state and up-regulate immune functions by binding to type I or type II receptors on the cells, and activating the JAK/STAT signal transduction pathway (Darnell et al., 1994).”
Background
The generation of PD-L1 and PD-L2 in cancer cells: From nuclear chromatin reorganization to extracellular presentation
Fan, Z., Wu, C., Chen, M., Jiang, Y., Wu, Y., Mao, R., & Fan, Y. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.09.010 · Cited by 120
STAT3 Regulation of Glioblastoma Pathogenesis
de la Iglesia, N., Puram, S. V., & Bonni, A. (2009) · Current Molecular Medicine · doi:10.2174/156652409788488739 · Cited by 117
Regulation of innate immune functions by guanylate-binding proteins
Praefcke, G. J. K. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.10.013 · Cited by 116
Erythropoietin and Its Angiogenic Activity
Kimáková, P., Solár, P., Solárová, Z., Komel, R., & Debeljak, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071519 · Cited by 124
“Formation of the complex EPO/EPOR results in the activation of proteins involved in basic signal transduction [5] such as Janus kinase 2 (JAK-2) and signal transducer and activator of transcription (STAT) [6], and of other signal pathways that control proliferation, survival of cells, and gene expression [7].”
Background
Neuroimmunology of the Interleukins 13 and 4
Mori, S., Maher, P. A., & Conti, B. (2016) · Brain Sciences · doi:10.3390/brainsci6020018 · Cited by 125
“Upon activation of IL-13Rα1, Stat1, 3, and 6 are phosphorylated and form a homodimer that migrates to the nucleus and binds to N6-GAS to drive transcription [31,42,44,45].”
Background
Bovine pretransfer endometrium and embryo transcriptome fingerprints as predictors of pregnancy success after embryo transfer
Salilew‐Wondim, D., Hoelker, M., Rings, F., Ghanem, N., Ulas-Cinar, M., Peippo, J., Tholen, E., Looft, C., Schellander, K., & Tesfaye, D. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00047.2010 · Cited by 121
Comparison of Macrophage Antimicrobial Responses Induced by Type II Interferons of the Goldfish (Carassius auratus L.)
Grayfer, L., García-García, E., & Belosevic, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096925 · Cited by 125
Hepatitis delta virus inhibits alpha interferon signaling #
Pugnale, P., Pazienza, V., Guilloux, K., & Negro, F. (2008) · Hepatology · doi:10.1002/hep.22654 · Cited by 114
Tumor Microenvironment Promotes Cancer Progression, Metastasis, and Therapeutic Resistance
Sung, S., Hsieh, C., Wu, D., Chung, L. W. K., & Johnstone, P. A. S. (2007) · Current Problems in Cancer · doi:10.1016/j.currproblcancer.2006.12.002 · Cited by 106
JAK inhibitor selectivity: new opportunities, better drugs?
Virtanen, A. T., Spinelli, F. R., Telliez, J., O’Shea, J. J., Silvennoinen, O., & Gadina, M. (2024) · Nature Reviews Rheumatology · doi:10.1038/s41584-024-01153-1 · Cited by 131
“The combination of four JAKs and seven STATs results in a complex web of signals, ultimately regulating various cellular functions 9 .”
The Process and Regulatory Components of Inflammation in Brain Oncogenesis
Mostofa, A., Punganuru, S. R., Madala, H. R., Al-Obaide, M., & Srivenugopal, K. S. (2017) · Biomolecules · doi:10.3390/biom7020034 · Cited by 121
“For instance, IFN activate the STAT-1-mediated transformation whereas IL-6 induces the STAT3 activity [95,96].”
Background
3C pro of Foot-and-Mouth Disease Virus Antagonizes the Interferon Signaling Pathway by Blocking STAT1/STAT2 Nuclear Translocation
Du, Y., Bi, J., Liu, J., Liu, X., Wu, X., Jiang, P., Yoo, D., Zhang, Y., Wu, J., Wan, R., et al. (2014) · Journal of Virology · doi:10.1128/jvi.03668-13 · Cited by 108
“Once activation is triggered by IFN, STAT1 and STAT2 form a heterodimer and associate with IRF9 to assemble the ISGF3 complex (11, 35).”
Background
Interferon-sensitive response element (ISRE) is mainly responsible for IFN-α-induced upregulation of programmed death-1 (PD-1) in macrophages
Cho, H.-Y., Lee, S.-W., Seo, S., Choi, I., Choi, I., & Lee, S.-W. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.08.003 · Cited by 104
Natural Products as a Potential Modulator of Microglial Polarization in Neurodegenerative Diseases
Jin, X., Liu, M.-Y., Zhang, D.-F., Zhong, X., Du, K., Qian, P., Gao, H., & Wei, M.-J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104253 · Cited by 109
Chromatin bridges, not micronuclei, activate cGAS after drug-induced mitotic errors in human cellsPreprint
Flynn, P. J., Koch, P., & Mitchison, T. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1101/2021.02.02.429360 · Cited by 110
“To confirm IFN secretion by BJ cells, we stimulated the cells with cGAMP and then stained for STAT1 phosphorylation, a canonical marker of IFN signaling (Darnell et al., 1994).”
Method
Repurposing Drugs, Ongoing Vaccine, and New Therapeutic Development Initiatives Against COVID-19
Saha, R. P., Sharma, A. R., Singh, M. K., Samanta, S., Bhakta, S., Mandal, S., Bhattacharya, M., Lee, S. S., & Chakraborty, C. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01258 · Cited by 118
STAT4: an immunoregulator contributing to diverse human diseases
Yang, C., Mai, H., Peng, J., Zhou, B., Hou, J., & Jiang, D. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.41852 · Cited by 137
Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling
Zuo, Y., Feng, Q., Jin, L., Huang, F., Miao, Y., Liu, J., Xu, Y., Chen, X., Zhang, H., Guo, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14948-z · Cited by 115
Stat3 promotes directional cell migration by regulating Rac1 activity via its activator βPIX
Teng, T., Lin, B., Manser, E., Ng, D. C. H., & Cao, X. (2009) · Journal of Cell Science · doi:10.1242/jcs.057109 · Cited by 99
“The signal transducers and activators of transcription (STATs) were identified as latent cytoplasmic transcription factors that are activated by cytokines and growth factors to mediate essential cellular processes such as cell growth, proliferation and immune responses (Darnell et al., 1994).”
Background
Porcine Reproductive and Respiratory Syndrome Virus Nsp1β Inhibits Interferon-Activated JAK/STAT Signal Transduction by Inducing Karyopherin-α1 Degradation
Wang, R., Nan, Y., Yu, Y., & Zhang, Y. (2013) · Journal of Virology · doi:10.1128/jvi.02643-12 · Cited by 125
Interleukin-4/STAT6 Represses STAT1 and NF-κB-dependent Transcription through Distinct Mechanisms
Ohmori, Y., & Hamilton, T. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006227200 · Cited by 106
Roles and functions of SARS-CoV-2 proteins in host immune evasion
Rashid, F., Xie, Z., Suleman, M., Shah, A., Khan, S., & Luo, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940756 · Cited by 140
“After activation, STAT1 and STAT2 are phosphorylated (24, 25).”
Background
Melatonin stabilizes rupture‐prone vulnerable plaques via regulating macrophage polarization in a nuclear circadian receptor RORα‐dependent manner
Ding, S. Z., Lin, N., Sheng, X., Zhao, Y., Su, Y., Xu, L., Tong, R., Yang, Y., Fu, Y., He, J., et al. (2019) · Journal of Pineal Research · doi:10.1111/jpi.12581 · Cited by 113
Novel mechanisms to inhibit HIV reservoir seeding using Jak inhibitors
Gavegnano, C., Brehm, J. H., Dupuy, F. P., Talla, A., Ribeiro, S. P., Kulpa, D. A., Cameron, C., Santos, S., Hurwitz, S. J., Marconi, V. C., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006740 · Cited by 112
“Since γ-C cytokines promote the activation of the Jak-STAT pathway (Fig 1) [8, 9, 11], paracrine or autocrine inhibition of IL-2, IL-7, and IL-15 induced signaling by ruxolitinib could be in part responsible for the inhibitory effects exerted by this compound on p24 production.”
Background
Resveratrol Potentiates the Cytotoxic Oxidative Stress Induced by Chemotherapy in Human Colon Cancer Cells
Santandreu, F. M., Valle, A., Oliver, J., & Roca, P. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000331733 · Cited by 115
Cooperativity of the MUC1 oncoprotein and STAT1 pathway in poor prognosis human breast cancer
Khodarev, N. N., Ahmad, R., Rajabi, H. N., Pitroda, S. P., Kufe, T., McClary, C., Joshi, M. D., MacDermed, D. M., Weichselbaum, R., & Kufe, D. W. (2009) · Oncogene · doi:10.1038/onc.2009.391 · Cited by 102
Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation
Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108
Toosendanin demonstrates promising antitumor efficacy in osteosarcoma by targeting STAT3
Zhang, T., Li, J., Yin, F., Lin, B., Wang, Z., Xu, J., Wang, H., Zuo, D., Wang, G., Hua, Y., et al. (2017) · Oncogene · doi:10.1038/onc.2017.270 · Cited by 132
The Role of STAT Signaling Pathways in the Pathogenesis of Systemic Lupus Erythematosus
Goropevšek, A., Holcar, M., & Avčin, T. (2016) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-016-8550-y · Cited by 113
“STAT proteins were first identified in 1992 as DNAbinding proteins, major components in IFN-dependent gene expression [18].”
Background
Two Naturally Occurring Terpenes, Dehydrocostuslactone and Costunolide, Decrease Intracellular GSH Content and Inhibit STAT3 Activation
Butturini, E., Cavalieri, E., de Prati, A. C., Darra, E., Rigo, A., Shoji, K., Murayama, N., Yamazaki, H., Watanabe, Y., Suzuki, H., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020174 · Cited by 104
“The Janus kinases (JAKs) and signal transducers and activators of transcription (STATs) pathway is responsible for signal transduction of a large number of cytokines and growth factors that regulate responses to inflammation or immune challenge and address the future of cell decision during development and neoplastic…”
Background
Regulation and function of interferon regulatory factors of Atlantic salmon
Bergan, V., Kileng, Ø., Sun, B., & Robertsen, B. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.04.015 · Cited by 99
Regulation of dendritic cell maturation and function by Bruton's tyrosine kinase via IL-10 and Stat3
Kawakami, Y., Inagaki, N., Salek‐Ardakani, S., Kitaura, J., Tanaka, H., Nagao, K., Kawakami, Y., Xiao, W., Nagai, H., Croft, M., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509784103 · Cited by 93
Pin1 is required for the Ser727 phosphorylation-dependent Stat3 activity
Lufei, C., Koh, T. H., Uchida, T., & Cao, X. (2007) · Oncogene · doi:10.1038/sj.onc.1210567 · Cited by 106
“Tyr-phosphorylation of Stat3 leads to dimerization via reciprocal interaction between the SH2 domain and the phosphorylated Tyr705, then nuclear transport, DNA binding and regulation of target gene expression (Darnell et al., 1994).”
Background
Phase I study of OPB ‐51602, an oral inhibitor of signal transducer and activator of transcription 3, in patients with relapsed/refractory hematological malignancies
Ogura, M., Uchida, T., Terui, Y., Hayakawa, F., Kobayashi, Y., Taniwaki, M., Takamatsu, Y., Naoe, T., Tobinai, K., Munakata, W., et al. (2015) · Cancer Science · doi:10.1111/cas.12683 · Cited by 110
Icaritin Inhibits JAK/STAT3 Signaling and Growth of Renal Cell Carcinoma
Li, S., Priceman, S. J., Xin, H., Zhang, W., Deng, J., Liu, Y., Huang, J., Zhu, W., Chen, M., Hu, W., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081657 · Cited by 117
“Many tumor-derived factors, such as IL10, IL-6 and VEGF that are crucial for both tumor growth and immunosuppression, activate STAT3 to create an efficient ‘‘feedforward’’ loop to induce persistent STAT3 activity in tumor cells and the tumor microenvironment [19,23,24,25].”
6-Bromoindirubin-3′-Oxime Inhibits JAK/STAT3 Signaling and Induces Apoptosis of Human Melanoma Cells
Liu, L., Nam, S., Tian, Y., Yang, F., Wu, J., Wang, Y., Scuto, A., Polychronopoulos, P., Magiatis, P., Skaltsounis, A., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3852 · Cited by 109
Signal transducer and activator of transcription 3 inhibitors: a patent review
Page, B. D. G., Ball, D. P., & Gunning, P. T. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.539205 · Cited by 103
“Unactivated Stat3 protein (either monomeric [6,9] or dimeric [10-12]) is then recruited to phosphorylated sites on the receptor via its phosphotyrosine (pY)-binding Src Homology 2 (SH2) domain.”
A novel form of human STAT1 deficiency impairing early but not late responses to interferons
Kong, X., Ciancanelli, M. J., Al-Hajjar, S. H., Alsina, L., Zumwalt, T. J., Bustamante, J. C., Feinberg, J. M., Audry, M., Prando, C., Bryant, V. L., et al. (2010) · Blood · doi:10.1182/blood-2010-04-280586 · Cited by 115
Challenges of the Immunotherapy: Perspectives and Limitations of the Immune Checkpoint Inhibitor Treatment
Dobosz, P., Stępień, M., Golke, A., & Dzieciątkowski, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052847 · Cited by 114
“However, on the other hand, the same molecule induces chemokine production, such as CXCL9 and CXCL10, influencing the number of the immune cells infiltrating the tumour, as well as triggering a proapoptotic effect, directly contributing to the programmed death of the cancer cells [24,26,27].”
Background
Signal transducer and activator of transcription 3 is involved in the cardioprotective signalling pathway activated by insulin therapy at reperfusion
Fuglesteg, B. N., Suleman, N., Tiron, C. E., Kanhema, T., Lacerda, L., Andreasen, T. V., Sack, M. N., Jonassen, A. K., Mjøs, O. D., Opie, L. H., et al. (2008) · Basic Research in Cardiology · doi:10.1007/s00395-008-0728-x · Cited by 100
“The Janus activated kinase (JAK) and Signal Transducer and Activator of Transcription 3 (STAT3) signalling pathway is responsive to a large number of cytokines, growth factors and hormones [6, 7, 18], and is known to play a vital role in cardioprotection related to ischemia-reperfusion (I/R) injury [2, 13, 16, 24, 26,…”
The Molecular Basis of Viral Inhibition of IRF- and STAT-Dependent Immune Responses
Chiang, H.-S., & Liu, H. M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2018.03086 · Cited by 108
“ISGF3 and GAF complexes then translocate into the nucleus mediated by importins and recruit additional coactivators, such as CREB binding protein (CBP)/p300 on the IFN-stimulated response element (ISRE)- or gamma IFN activated sequence (GAS)-containing promoters to stimulate expression of a distinct group of ISGs.”
Background
Novel Therapies for Diabetic Kidney Disease
Alicic, R. Z., & Tuttle, K. R. (2014) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2014.01.007 · Cited by 110
The effect of STAT3 inhibition on status epilepticus and subsequent spontaneous seizures in the pilocarpine model of acquired epilepsy
Grabenstatter, H. L., Angel, Y. C. D., Carlsen, J., Wempe, M. F., White, A. M., Cogswell, M., Russek, S. J., & Brooks‐Kayal, A. R. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.09.003 · Cited by 109
The Nonstructural Proteins of Nipah Virus Play a Key Role in Pathogenicity in Experimentally Infected Animals
Yoneda, M., Guillaume, V., Sato, H., Fujita, K., Georges-Courbot, M., Ikeda, F., Omi, M., Muto-Terao, Y., Wild, T., & Kai, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012709 · Cited by 104
“. Type I IFNs mediate their biological functions by binding to the receptor on the target cells, resulting in autophosphorylation and activation of the Janus kinases (JAKs), JAK1 and tyrosine kinase 2, leading to phosphorylation of the signaling molecules STAT1 and STAT2”
Background
Mast cell homeostasis and the JAK–STAT pathway
Morales, J. K., Falanga, Y. T., Depcrynski, A., Fernando, J. F. A., & Ryan, J. J. (2010) · Genes and Immunity · doi:10.1038/gene.2010.35 · Cited by 110
Viral manipulation of STAT3: Evade, exploit, and injure
Suarez, A. A. R., Renne, N. V., Baumert, T. F., & Lupberger, J. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006839 · Cited by 112
Signal transducer and activator of transcription 3 activation is associated with bladder cancer cell growth and survival
Chen, C.-L., Cen, L., Kohout, J., Hutzen, B., Chan, C., Hsieh, F.-C., Loy, A., Huang, V., Cheng, G., & Lin, J. (2008) · Molecular Cancer · doi:10.1186/1476-4598-7-78 · Cited by 125
“DnStat3 may inhibit phosphorylation and dimerization of endogenous Stat3 [22-24] and down regulates a group of survival and proliferation genes [2527].”
Background
IL‐6–induced cGGNBP2 encodes a protein to promote cell growth and metastasis in intrahepatic cholangiocarcinoma
Li, H., Lan, T., Liu, H., Liu, C., Dai, J., Xu, L., Cai, Y., Hou, G., Xie, K., Liao, M., et al. (2021) · Hepatology · doi:10.1002/hep.32232 · Cited by 124
“[24,25] Because phosphorylation is required for STAT3 nuclear translocation and transcriptional activity,[26] we then investigated whether cGGNBP2184aa regulated STAT3 phosphorylation.”
Background
A protein interaction network associated with asthma
Hwang, S., Son, S., Kim, S. C., Kim, Y., Jeong, H., & Lee, D. (2008) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2008.02.011 · Cited by 100
Distinct mechanisms of loss of IFN-gamma mediated HLA class I inducibility in two melanoma cell lines
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“and IFN-γ R2, which are intracellularly associated with Jak-1 and Jak-2, respectively [1,8].”
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“For treatment with AS-IV (100mM), cells were incubated for 24 h after BMDM treated with PBS, LPS + IFN-g, or IL-4.”
BackgroundInfluential

Authors: Darnell, J. E., Kerr, L. M., & Stark, G. R.
Affiliations: Rockefeller University (US)
Case Comprehensive Cancer Center (US)
ORCID: Stark, George R.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-06-03
Volume: 264
Issue: 5164
Pages: 1415-1421
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8197455
OpenAlex: W2029275361
Cited by: 6,080
References: 85
Citations by year: 2026: 84 · 2025: 139 · 2024: 175 · 2023: 170 · 2022: 183 · 2021: 177 · 2020: 162 · 2019: 155 · 2018: 121 · 2017: 166 · 2016: 148 · 2015: 152 · 2014: 160 · 2013: 207 · 2012: 188
FWCI: 28.59
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: JAK/STAT signaling, interferon-alpha, interferon-gamma, signal transduction, STAT proteins, transcriptional activation, JAK kinases, interferon receptor, nuclear translocation, DNA binding
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA-Binding Proteins, Genes, Genetic Complementation Test, Humans, Interferon-gamma, Molecular Sequence Data, Mutation, Protein-Tyrosine Kinases, Regulatory Sequences, Nucleic Acid, Transcription Factors, Signal Transduction, Transcriptional Activation, Interferon-alpha, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

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