Cited by 814Cytokine Signaling Pathways and InteractionsNF-κB Signaling Pathwaysinterferon and immune responses

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Association of Transcription Factor APRF and Protein Kinase Jak1 with the Interleukin-6 Signal Transducer gp130

Lütticken, Claudia, Wegenka, Ursula M., Yuan, Juping, Buschmann, Jan, Schindler, Chris, Ziemiecki, Andrew, Harpur, Ailsa G., Wilks, Andrew F., Yasukawa, Kiyoshi, Taga, Tetsuya, Kishimoto, Tadamitsu, Barbieri, Giovanna, Pellegrini, Sandra, Sendtner, Michael, Heinrich, Peter C., Horn, Friedemann·1994·Science

DOI 10.1126/science.8272872

Open this paper in CoChat — free account

Abstract

Interleukin-6 (IL-6), leukemia inhibitory factor, oncostatin M, interleukin-11, and ciliary neurotrophic factor bind to receptor complexes that share the signal transducer gp130. Upon binding, the ligands rapidly activate DNA binding of acute-phase response factor (APRF), a protein antigenically related to the p91 subunit of the interferon-stimulated gene factor-3α (ISGF-3α). These cytokines caused tyrosine phosphorylation of APRF and ISGF-3α p91. Protein kinases of the Jak family were also rapidly tyrosine phosphorylated, and both APRF and Jak1 associated with gp130. These data indicate that Jak family protein kinases may participate in IL-6 signaling and that APRF may be activated in a complex with gp130.

Integrity signals

Registry

Crossref · 10.1126/science.8272872

Cites

0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Interferon-alpha regulates nuclear translocation and DNA-binding affinity of ISGF3, a multimeric transcriptional activator.
Kessler, D. S., Veals, S. A., Fu, X. Y., & Levy, D. E. (1990) · Genes & Development · doi:10.1101/gad.4.10.1753 · Cited by 312

Flagged first, then by citations

Show all 0 references

Research works printed but not linked: 30

10.1016/0092-8674(93)90415-M · DOI
BAZAN, J.F., NEUROPOIETIC CYTOKINES IN THE HEMATOPOIETIC FOLD, NEURON 7: 197 (1991). · DOI
BAZAN, J.F., STRUCTURAL DESIGN AND MOLECULAR EVOLUTION OF A CYTOKINE RECEPTOR SUPERFAMILY, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 87: 6934 (1990).
COOPER, J.A., DETECTION AND QUANTIFICATION OF PHOSPHOTYROSINE IN PROTEINS, METHODS IN ENZYMOLOGY 99: 387 (1983). · DOI
10.1126/science.8390097 · DOI
DECKER, T, CYTOPLASMIC ACTIVATION OF GAF, AN IFN-GAMMA-REGULATED DNA-BINDING FACTOR, EMBO JOURNAL 10: 927 (1991). · DOI
FIRMBACHKRAFT, I, TYK2, PROTOTYPE OF A NOVEL CLASS OF NONRECEPTOR TYROSINE KINASE GENES, ONCOGENE 5: 1329 (1990).
FU, X.Y., TRANSCRIPTION FACTOR P91 INTERACTS WITH THE EPIDERMAL GROWTH-FACTOR RECEPTOR AND MEDIATES ACTIVATION OF THE C-FOS GENE PROMOTER, CELL 74: 1135 (1993). · DOI
10.1126/science.1542794 · DOI
HIBI, M, MOLECULAR-CLONING AND EXPRESSION OF AN IL-6 SIGNAL TRANSDUCER, GP130, CELL 63: 1149 (1990). · DOI · Paper page
Hibi, M., Cell 63: 1149 (1990). · DOI · Paper page
10.1126/science.8378773 · DOI
10.1126/science.8511589 · DOI
PATTERSON, P.H., NEURONAL DIFFERENTIATION FACTORS CYTOKINES AND SYNAPTIC PLASTICITY, CELL 72: 123 (1993). · DOI
PELLEGRINI, S, EARLY EVENTS IN SIGNALING BY INTERFERONS, TRENDS IN BIOCHEMICAL SCIENCES 18: 338 (1993). · DOI
10.1126/science.8378774 · DOI
10.1126/science.8397445 · DOI
SCHINDLER, C, PROTEINS OF TRANSCRIPTION FACTOR ISGF-3 - ONE GENE ENCODES THE 91-KDA AND 84-KDA ISGF-3 PROTEINS THAT ARE ACTIVATED BY INTERFERON-ALPHA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 7836 (1992).
10.1126/science.1496401 · DOI · Paper page
10.1126/science.1281555 · DOI
10.1126/science.7690989 · DOI · Paper page
SILVENNOINEN, O, STRUCTURE OF THE MURINE JAK2 PROTEIN-TYROSINE KINASE AND ITS ROLE IN INTERLEUKIN-3 SIGNAL-TRANSDUCTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 8429 (1993).
STAHL, N, THE ALPHAS, BETAS, AND KINASES OF CYTOKINE RECEPTOR COMPLEXES, CELL 74: 587 (1993). · DOI
10.1016/0092-8674(92)90105-L · DOI
WEGENKA, U.M., ACUTE-PHASE RESPONSE FACTOR, A NUCLEAR FACTOR BINDING TO ACUTE-PHASE RESPONSE ELEMENTS, IS RAPIDLY ACTIVATED BY INTERLEUKIN-6 AT THE POSTTRANSLATIONAL LEVEL, MOLECULAR AND CELLULAR BIOLOGY 13: 276 (1993).
WILKS, A.F., 2 NOVEL PROTEIN-TYROSINE KINASES, EACH WITH A 2ND PHOSPHOTRANSFERASE-RELATED CATALYTIC DOMAIN, DEFINE A NEW CLASS OF PROTEIN-KINASE, MOLECULAR AND CELLULAR BIOLOGY 11: 2057 (1991).
WITTHUHN, B.A., JAK2 ASSOCIATES WITH THE ERYTHROPOIETIN RECEPTOR AND IS TYROSINE-PHOSPHORYLATED AND ACTIVATED FOLLOWING STIMULATION WITH ERYTHROPOIETIN, CELL 74: 227 (1993). · DOI
YOSHIMURA, A, INVITRO PHOSPHORYLATION OF THE ERYTHROPOIETIN RECEPTOR AND AN ASSOCIATED PROTEIN, PP130, MOLECULAR AND CELLULAR BIOLOGY 12: 706 (1992).
Yuan, J., Molecular and Cellular Biology 14: 1657 (1994).
Ip, N. Y., Cell 69: 1121 (1992). · DOI

Sorted by citations

Principles of interleukin (IL)-6-type cytokine signalling and its regulation
HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272
Self-citation
Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway
HEINRICH, P. C., BEHRMANN, I., MÜLLER-NEWEN, G., SCHAPER, F., & GRAEVE, L. (1998) · Biochemical Journal · doi:10.1042/bj3340297 · Cited by 2,130
Self-citation
Stat3: a STAT Family Member Activated by Tyrosine Phosphorylation in Response to Epidermal Growth Factor and Interleukin-6
Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070
Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice.
Bôle-Feysot, C., Goffin, V., Edery, M., Binart, N., & Kelly, P. (1998) · Endocrine reviews · doi:10.1210/edrv.19.3.0334 · Cited by 1,973
“IL-6-activated transcription factor (552).”
Self-renewal of pluripotent embryonic stem cells is mediated via activation of STAT3.Preprint
Niwa, H., Burdon, T., Chambers, I., & Smith, A. G. (1998) · Genes & Development · doi:10.1101/gad.12.13.2048 · Cited by 1,673
gp 130 AND THE INTERLEUKIN-6 FAMILY OF CYTOKINES
Taga, T., & Kishimoto, T. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.797 · Cited by 1,468
Self-citation
Interleukin-6 family of cytokines and gp130.
Kishimoto, T., Akira, S., Narazaki, M., & Taga, T. (1995) · Blood · doi:10.1182/blood.v86.4.1243.bloodjournal8641243 · Cited by 1,362
Self-citation
Transcriptional Regulation by Extracellular signals: Mechanisms and Specificity
Hill, C. S., & Treisman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90403-4 · Cited by 1,012
Roles of STAT3 in mediating the cell growth, differentiation and survival signals relayed through the IL-6 family of cytokine receptors
Hirano, T., Ishihara, K., & Hibi, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203551 · Cited by 1,207
“…of gp130 or heterodimerization of gp130 with other gp130-related receptors (LIF receptor b, OSM receptor a, and CT-1 receptor a), which results in the activation of the gp130-associated Janus kinases (JAK1, JAK2, and TYK2) (Lutticken et al., 1994; Matsuda et al., 1994; Stahl et al., 1994).”
Background
Embryonic stem cells
Rippon, H. J., & Bishop, A. E. (2004) · Cell Proliferation · doi:10.1111/j.1365-2184.2004.00298.x · Cited by 536
Regulation of gliogenesis in the central nervous system by the JAK-STAT signaling pathway.
Bonni, A., Sun, Y., Nadal-Vicens, M., Bhatt, A. S., Frank, D., Rozovsky, I., Stahl, N., Yancopouloš, G., & Greenberg, M. (1997) · Science · doi:10.1126/science.278.5337.477 · Cited by 1,050
Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
Akira, S., Nishio, Y., Inoue, M., Wang, X.-J., We, S., Matsusaka, T., Yoshida, K., Sudo, T., Naruto, M., & Kishimoto, T. (1994) · Cell · doi:10.1016/0092-8674(94)90235-6 · Cited by 1,019
Self-citation
Jaks and Stats in signaling by the cytokine receptor superfamily.
Ihle, J., & Kerr, I. (1995) · Trends in Genetics · doi:10.1016/s0168-9525(00)89000-9 · Cited by 953
Transcription factors: An overview
Latchman, D. S. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)00085-x · Cited by 856
What does Stat3 do?
Levy, D. E., & Lee, C. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15650 · Cited by 834
“IL-6–type cytokines evoke a number of distinct responses in different cells, including induction of an acute-phase response in hepatoma cells, stimulation of proliferation in B lymphocytes, activation of terminal differentiation and growth arrest in monocytes (11), and maintenance of the pluripotency of embryonic stem…”
BackgroundInfluential
The two faces of IL-6 on Th1/Th2 differentiation
Diehl, S. A., & Rincón, M. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(02)00210-9 · Cited by 873
Interleukin 6 and its receptor: ten years later
Hirano, T. (1998) · International Reviews of Immunology · doi:10.3109/08830189809042997 · Cited by 788
Cytoplasmic Signaling Pathways That Regulate Cardiac Hypertrophy
Molkentin, J. D., & Dorn, G. W. (2001) · Annual Review of Physiology · doi:10.1146/annurev.physiol.63.1.391 · Cited by 684
STAT3 signaling in immunity
Hillmer, E. J., Zhang, H., Li, H. S., & Watowich, S. S. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.05.001 · Cited by 740
What does Stat3 do?
Levy, D. E., & Lee, C.-K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215650 · Cited by 734
Interleukin-6 Family CytokinesPreprint
Rose‐John, S. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028415 · Cited by 846
“During the 1990s, intracellular signaling induced by activated gp130 was recognized to be mainly mediated by JAKs constitutively associated with the cytoplasmic portion of gp130, which led to the recruitment and activation of signal transducers and activators of transcription (STATs), which on phosphorylation by JAKs…”
BackgroundInfluential
Hepatic acetyl CoA links adipose tissue inflammation to hepatic insulin resistance and type 2 diabetes
Perry, R. J., Camporez, J.-P. G., Kursawe, R., Titchenell, P. M., Zhang, D., Perry, C. J., Jurczak, M. J., Abudukadier, A., Han, M. S., Zhang, X.-M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.012 · Cited by 719
“…HGP was associated with a 50% reduction in hepatic acetyl CoA concentrations within 10 min of the start of the insulin infusion as well as a 60% suppression of whole-body glycerol and palmitate turnover at steady state with no changes in plasma lactate, glucagon, or liver glycogen concentrations (”
Background
Mitochondrial STAT3 Supports Ras-Dependent Oncogenic Transformation
Gough, D. J., Corlett, A., Schlessinger, K., Wegrzyn, J., Larner, A. C., & Levy, D. E. (2009) · Science · doi:10.1126/science.1171721 · Cited by 716
Cytokine Signaling Through Nonreceptor Protein Tyrosine Kinases
Taniguchi, T. (1995) · Science · doi:10.1126/science.7716517 · Cited by 689
The soluble interleukin 6 receptor: mechanisms of production and implications in disease
Jones, S. A., Horiuchi, S., Topley, N., Yamamoto, N., & Fuller, G. M. (2001) · The FASEB Journal · doi:10.1096/fj.99-1003rev · Cited by 628
Interleukin‐3, granulocyte‐macrophage colony stimulating factor and interleukin‐5 transduce signals through two STAT5 homologs.
Mui, A., Wakao, H., O’Farrell, A.-M., Harada, N., & Miyajima, A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07100.x · Cited by 615
Signaling by the cytokine receptor superfamily: JAKs and STATs
Ihle, J. N., Witthuhn, B. A., Quelle, F. W., Yamamoto, K., Thierfelder, W. E., Kreider, B. L., & Silvennoinen, O. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90026-4 · Cited by 648
Signal Transducer and Activator of Transcription‐3, Inflammation, and Cancer
Aggarwal, B. B., Kunnumakkara, A. B., Harikumar, K. B., Gupta, S. R., Tharakan, S. T., Koca, C., Dey, S., & Sung, B. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04911.x · Cited by 663
Two Signals Are Necessary for Cell Proliferation Induced by a Cytokine Receptor gp130: Involvement of STAT3 in Anti-Apoptosis
Fukada, T., Hibi, M., Yamanaka, Y., Takahashi-Tezuka, M., Fujitani, Y., Yamaguchi, T., Nakajima, K., & Hirano, T. (1996) · Immunity · doi:10.1016/s1074-7613(00)80501-4 · Cited by 652
Interleukin-6–dependent survival of multiple myeloma cells involves the Stat3-mediated induction of microRNA-21 through a highly conserved enhancer
Löffler, D., Brocke-Heidrich, K., Pfeifer, G., Stocsits, C., Hackermüller, J., Kretzschmar, A. K., Burger, R., Gramatzki, M., Blumert, C., Bauer, K., et al. (2007) · Blood · doi:10.1182/blood-2007-03-081133 · Cited by 637
Self-citation
STAT3 Serine Phosphorylation by ERK-Dependent and -Independent Pathways Negatively Modulates Its Tyrosine Phosphorylation
Chung, J., Uchida, E., Grammer, T. C., & Blenis, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6508 · Cited by 620
“Once these growth factor or cytokine receptors are occupied by their ligands, tyrosine residues in the cytoplasmic domain of the receptors become phosphorylated by cytokine receptor-associated JAK family tyrosine kinases (19, 32) or by the growth factor-activated receptor tyrosine kinases (16, 26, 34).”
Background
Requirement of Serine Phosphorylation for Formation of STAT-Promoter Complexes
Zhang, X., Blenis, J., Li, H., Schindler, C., & Chen‐Kiang, S. (1995) · Science · doi:10.1126/science.7701321 · Cited by 573
Self-citation
JAK-STAT Signaling: A Double-Edged Sword of Immune Regulation and Cancer Progression
Owen, K. L., Brockwell, N. K., & Parker, B. S. (2019) · Cancers · doi:10.3390/cancers11122002 · Cited by 728
A central role for Stat3 in IL‐6‐induced regulation of growth and differentiation in M1 leukemia cells.
Nakajima, K., Yamanaka, Y., Nakae, K., Kojima, H., Ichiba, M., Kiuchi, N., Kitaoka, T., Fukada, T., Hibi, M., & Hirano, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00734.x · Cited by 565
Interleukin-6 in the Injured Patient
Biffl, W. L., Moore, E. E., Moore, F. A., & Peterson, V. M. (1996) · Annals of Surgery · doi:10.1097/00000658-199611000-00009 · Cited by 502
JAK–STAT pathway targeting for the treatment of inflammatory bowel disease
Salas, A., Hernández-Rocha, C., Duijvestein, M., Faubion, W. A., McGovern, D. P. B., Vermeire, S., Vetrano, S., & Casteele, N. V. (2020) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-020-0273-0 · Cited by 658
Differential Effects of Interleukin-6 and -10 on Skeletal Muscle and Liver Insulin Action In Vivo
Kim, H.-J., Higashimori, T., Park, S.-Y., Choi, H., Dong, J., Kim, Y.-J., Noh, H.-L., Cho, Y.-R., Cline, G., Kim, Y.-B., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.4.1060 · Cited by 534
Interleukin-6: Biology, signaling and strategies of blockade
Schaper, F., & Rose‐John, S. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.07.004 · Cited by 532
Janus kinases: components of multiple signaling pathways
Rane, S. G., & Reddy, E. P. (2000) · Oncogene · doi:10.1038/sj.onc.1203925 · Cited by 477
“JAK2 is activated following erythropoietin stimulation of its receptor (Witthuhn et al., 1993) while JAK1 and JAK2 have been implicated in signaling by IL-3, GM-CSF and IL-5 (Silvennoinen et al., 1993a; Quelle et al., 1994; Lutticken et al., 1994).”
Background
Frequent in-frame somatic deletions activate gp130 in inflammatory hepatocellular tumours
Rebouissou, S., Amessou, M., Couchy, G., Poussin, K., Imbeaud, S., Pilati, C., Izard, T., Balabaud, C., Bioulac-Sage, P., & Zucman-Rossi, J. (2009) · Nature · doi:10.1038/nature07475 · Cited by 477
Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3
Stein, T., Morris, J. S., Davies, C. R., Weber-Hall, S. J., Pringle, M. A., Heath, V. J., Bell, A. K., Ferrier, R. K., Sandilands, G. P., & Gusterson, B. A. (2003) · Breast Cancer Research · doi:10.1186/bcr753 · Cited by 382
Physical activity and modulation of systemic low-level inflammation
Bruunsgaard, H. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0505247 · Cited by 429
“IL-6 binds to the IL-6sR and the complex associates with two gp130 molecules for the initiation of intracellular signaling [171].”
Background
Identification and functional characterization of a second chain of the interleukin‐10 receptor complex
Kotenko, S. V., Krause, C. D., Izotova, L. S., Pollack, B. P., Wu, W., & Pestka, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.5894 · Cited by 382
“We showed that, if the IFN-γR2cytokines, IL-10 and IL-12 (Velazquez et al., 1992; Bacon et al., 1995; Barbieri et al., 1994; Lütticken et al., 1994; intracellular domain is replaced with the intracellular domains of other receptors, Hu-IFN-γR1, Hu-IFN-αR2c,Stahl et al., 1994; Finbloom and…”
Background
Essential role of STAT3 for embryonic stem cell pluripotency
Raz, R., Lee, C., Cannizzaro, L. A., D’Eustachio, P., & Levy, D. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2846 · Cited by 407
Interleukin (IL)-6 induction of osteoclast differentiation depends on IL-6 receptors expressed on osteoblastic cells but not on osteoclast progenitors.
Udagawa, N., Takahashi, N., Katagiri, T., Tamura, T., Wada, S., Findlay, D. M., Martin, T. J., Hirota, H., Taga, T., Kishimoto, T., et al. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.5.1461 · Cited by 410
“The JAK family of protein kinases (JAK1, JAK2, and TYK2) and the latent cytoplasmic transcription factor A P R F / S T A T 3 participate in IL-6 signaling (40, 50, 51).”
Self-citation
The chemokine SDF‐lα triggers CXCR4 receptor dimerization and activates the JAK/STAT pathway
Vila‐Coro, A. J., Rodrı́guez-Frade, J. M., de Ana, A. M., Moreno-Ortiz, M. C., Martínez‐A, C., & Mellado, M. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.13.1699 · Cited by 517
Multiple Routes to Astrocytic Differentiation in the CNS
Rajan, P., & McKay, R. D. G. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-10-03620.1998 · Cited by 388
“Signaling is initiated by members of the JAK family of tyrosine kinases, specifically Jak1, Jak2, and Tyk2 (Lutticken et al., 1994; Stahl et al., 1994).”
Background
Signaling mechanisms through gp130: A model of the cytokine system
Hirano, T., Nakajima, K., & Hibi, M. (1997) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(98)80005-1 · Cited by 375
Mice lacking the CNTF receptor, unlike mice lacking CNTF, exhibit profound motor neuron deficits at birth.
Dechiara, T., Vejsada, R., Poueymirou, W., Acheson, A., Suri, C., Conover, J., Friedman, B., Mcclain, J., Pan, L., Stahl, N., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90172-8 · Cited by 395
SOCS3 Exerts Its Inhibitory Function on Interleukin-6 Signal Transduction through the SHP2 Recruitment Site of gp130
Schmitz, J., Weissenbach, M., Haan, S., Heinrich, P. C., & Schaper, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12848 · Cited by 388
Self-citation
Interleukin‐6: Structure‐function relationships
Simpson, R. J., Hammacher, A., Smith, D. K., Matthews, J. M., & Ward, L. D. (1997) · Protein Science · doi:10.1002/pro.5560060501 · Cited by 372
Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways.
Ueda, T., Bruchovsky, N., & Sadar, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108255200 · Cited by 381
Hepatic acute phase proteins – Regulation by IL-6- and IL-1-type cytokines involving STAT3 and its crosstalk with NF-κB-dependent signaling
Bode, J. G., Albrecht, U., Häussinger, D., Heinrich, P. C., & Schaper, F. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.008 · Cited by 379
Self-citation
Inhibition of constitutively active Stat3 suppresses proliferation and induces apoptosis in glioblastoma multiforme cells
Rahaman, S. O., Harbor, P. C., Chernova, O., Barnett, G. H., Vogelbaum, M. A., & Haque, S. J. (2002) · Oncogene · doi:10.1038/sj.onc.1206047 · Cited by 377
“IL-6 activates Stat3 through the activation of gp130 that is associated with Jak1, Jak2 or Tyk2 (Lutticken et al., 1994; Stahl et al., 1994).”
Background
Tracking STAT nuclear traffic
Reich, N. C., & Liu, L. (2006) · Nature Reviews Immunology · doi:10.1038/nri1885 · Cited by 376
“Nuclear STAT3 independent of phosphorylation STAT3 was first identified as a DNA-binding factor that is activated by IL-6 to regulate gene expression in the acute-phase inflammatory respons”
Background
Cardiotrophin-1
Pennica, D., Shaw, K. J., Swanson, T. A., Moore, M. W., Shelton, D. L., Zioncheck, K., Rosenthal, A., Taga, T., Paoni, N. F., & Wood, W. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10915 · Cited by 435
Self-citation
Historical overview of the interleukin-6 family cytokine
Kang, S., Narazaki, M., Metwally, H., & Kishimoto, T. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20190347 · Cited by 360
Self-citation
Activation of STAT3 by IL-6 and IL-10 in primary human macrophages is differentially modulated by suppressor of cytokine signaling 3
Niemand, C., Nimmesgern, A., Haan, S., Fischer, P., Schaper, F., Rossaint, R., Heinrich, P. C., & Müller-Newen, G. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.6.3263 · Cited by 357
Self-citation
Differential Activation of Acute Phase Response Factor/STAT3 and STAT1 via the Cytoplasmic Domain of the Interleukin 6 Signal Transducer gp130
Gerhartz, C., Heesel, B., Sasse, J., Hemmann, U., Landgraf, C., Schneider‐Mergener, J., Horn, F., Heinrich, P. C., & Graeve, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12991 · Cited by 311
Self-citation
Obesity-Induced TNFα and IL-6 Signaling: The Missing Link between Obesity and Inflammation—Driven Liver and Colorectal Cancers
Kern, L., Mittenbühler, M., Vesting, A., Ostermann, A., Wunderlich, C., & Wunderlich, F. (2018) · Cancers · doi:10.3390/cancers11010024 · Cited by 331
STAT3 Activation in Stromal/Osteoblastic Cells Is Required for Induction of the Receptor Activator of NF-κB Ligand and Stimulation of Osteoclastogenesis by gp130-utilizing Cytokines or Interleukin-1 but Not 1,25-Dihydroxyvitamin D3 or Parathyroid Hormone*
O'Brien, C. A., Gubrij, I., Lin, S.-C., Saylors, R., & Manolagas, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.19301 · Cited by 326
Regulation of STAT‐dependent pathways by growth factors and cytokines
Leaman, D. W., Leung, S., Li, X.-X., & Stark, G. R. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.14.9002549 · Cited by 318
“For example, JAK1, JAK2, and Tyk2 can all be phosphorylated in response to IL-6, depending on the cell type used (17, 18).”
The Structure, Regulation and Function of the Janus Kinases (JAKs) and the Signal Transducers and Activators of Transcription (STATs)
Pellegrini, S., & Dusanter‐Fourt, I. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00615.x · Cited by 285
Self-citation
Dual Oncostatin M (OSM) Receptors
Mosley, B., Imus, C. D., Friend, D., Boiani, N., Thoma, B., Park, L., & Cosman, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32635 · Cited by 307
Role of STAT2 in the Alpha Interferon Signaling Pathway
Leung, S., Qureshi, S. A., Kerr, I. M., Darnell, J. E., Jr., & Stark, G. R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1312 · Cited by 279
“The same two factors are also activated in response to IL-6 (23).”
Background
The Jak-Stat Pathway: Cytokine Signalling from the Receptor to the Nucleus
Heim, M. H. (1999) · Journal of Receptors and Signal Transduction · doi:10.3109/10799899909036638 · Cited by 275
A Kaposi's Sarcoma-associated Herpesvirus-encoded Cytokine Homolog (vIL-6) Activates Signaling through the Shared gp130 Receptor Subunit
Molden, J., Chang, Y., You, Y., Moore, P. S., & Goldsmith, M. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19625 · Cited by 281
Targeting Stat3 in cancer therapy
Jing, N., & Tweardy, D. J. (2005) · Anti-Cancer Drugs · doi:10.1097/00001813-200507000-00002 · Cited by 281
Dissection of signaling cascades through gp130 in vivo: reciprocal roles for STAT3- and SHP2-mediated signals in immune responses.
Ohtani, T., Ishihara, K., Atsumi, T., Nishida, K., Kaneko, Y., Miyata, T., Itoh, S., Narimatsu, M., Maeda, H., Fukada, T., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80162-4 · Cited by 284
“…SHP2- and STAT3-mediated signals generated from family cytokines to their receptors activates Janus ki- gp130 in vivo, we generated a series of knockin mouse nases (JAK1, JAK2, and TYK2) (Lutticken et al., 1994; lines, in which the SHP2- and/or STAT3-mediated sig- nals are specifically disrupted.”
Background
Multiple Myeloma: Increasing Evidence for a Multistep Transformation Process
Hallek, M. J., Bergsagel, P. L., & Anderson, K. C. (1998) · Blood · doi:10.1182/blood.v91.1.3 · Cited by 750
JAKs, STATs and Src kinases in hematopoiesis
Rane, S. G., & Reddy, E. P. (2002) · Oncogene · doi:10.1038/sj.onc.1205398 · Cited by 245
“…of hematopoietic cells appears to result predominantly in the activation of JAK2, although JAK1 and TYK-2 have also been found to be activated in certain cell systems (Silvennoinen et al., 1993a,b; Quelle et al., 1994; Lutticken et al., 1994; Chaturvedi et al., 1997, 1998; Jaster et al., 1997).”
Background
IL-6 signal transduction and its physiological roles: the signal orchestration model
Kamimura, D., Ishihara, K., & Hirano, T. (2003) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/s10254-003-0012-2 · Cited by 673
“gp130 constitutively associates with JAK1, JAK2, and TYK2 (Lutticken et al. 1994; Narazaki et al. 1994; Stahl et al. 1994).”
Background
Novel neurotrophin-1/B cell-stimulating factor-3: A cytokine of the IL-6 family
Senaldi, G., Varnum, B. C., Sarmiento, U. M., Starnes, C. O., Lile, J., Scully, S. A., Guo, J., Elliott, G., McNinch, J. S., Shaklee, C. L., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11458 · Cited by 253
Dominant Negative Stat3 Mutant Inhibits Interleukin-6-induced Jak-STAT Signal Transduction
Kaptein, A., Paillard, V., & Saunders, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.5961 · Cited by 251
Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3'-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells.
Qiu, Y., Robinson, D., Pretlow, T., & Kung, H. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.7.3644 · Cited by 258
Interleukin-6 Inhibits Transforming Growth Factor-β-induced Apoptosis through the Phosphatidylinositol 3-Kinase/Akt and Signal Transducers and Activators of Transcription 3 Pathways
Chen, R., Chang, M.-C., Su, Y., Tsai, Y.-T., & Kuo, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23013 · Cited by 224
Regulation of autophagy by stress-responsive transcription factors
Pietrocola, F., Izzo, V., Niso‐Santano, M., Vacchelli, E., Galluzzi, L., Maiuri, M. C., & Kroemer, G. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.05.008 · Cited by 277
gp130 at the nexus of inflammation, autoimmunity, and cancer
Silver, J. S., & Hunter, C. A. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0410217 · Cited by 260
“Under normal circumstances, the Janus kinases JAK1, JAK2, and tyrosine kinase 2 are constitutively associated with gp130, but receptor engagement leads to their phosphorylation and activation [17, 18].”
Background
HBx Protein of Hepatitis B Virus Activates Jak1-STAT Signaling
Lee, Y., & Yun, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25510 · Cited by 239
The tripartite CNTF receptor complex: activation and signaling involves components shared with other cytokines.
Stahl, N., & Yancopouloš, G. (1994) · Journal of Neurobiology · doi:10.1002/neu.480251111 · Cited by 254
Characterization of the role of IL‐6 in the progression of prostate cancer
Chung, T., Yu, J.-Q., Spiotto, M., Bartkowski, M., & Simons, J. (1999) · The Prostate · doi:10.1002/(sici)1097-0045(19990215)38:3 · Cited by 253
Stat3 protects against Fas-induced liver injury by redox-dependent and -independent mechanisms
Haga, S., Terui, K., Zhang, H. Q., Enosawa, S., Ogawa, W., Inoue, H., Okuyama, T., Takeda, K., Akira, S., Ogino, T., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17970 · Cited by 237
“Stat3 was first described as a molecule with DNA-binding activity, found in IL-6–stimulated hepatocytes, that was capable of selectively interacting with an enhancer element in the promoter of acute-phase genes known as the acute-phase response element (6, 7).”
Background
JAK/STAT signaling by cytokine receptors
Liu, K. D., Gaffen, S. L., & Goldsmith, M. A. (1998) · Current Opinion in Immunology · doi:10.1016/s0952-7915(98)80165-9 · Cited by 237
Differences in Wound Healing in Mice with Deficiency of IL-6 versus IL-6 Receptor
McFarland-Mancini, M. M., Funk, H. M., Paluch, A. M., Zhou, M., Giridhar, P. V., Mercer, C. A., Kozma, S. C., & Drew, A. F. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901929 · Cited by 249
“The Janus family kinases, JAK1, JAK2, and TYK2, are constitutively associated with the cytoplasmic tail of gp130 and phosphorylate gp130 dimers (6, 7).”
Background
Roles of JAKs in Activation of STATs and Stimulation of c- fos Gene Expression by Epidermal Growth Factor
Leaman, D. W., Pisharody, S., Flickinger, T. W., Commane, M., Schlessinger, J., Kerr, I. M., Levy, D. E., & Stark, G. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.1.369 · Cited by 226
“For example, interleukin 6, CNTF, and OSM, all of which use a common gp130 receptor subunit, activate multiple JAK proteins which differ depending on the cell line examined (38, 63).”
Background
An Indispensable Role for STAT1 in IL-27-Induced T-bet Expression but Not Proliferation of Naive CD4+ T Cells
Kamiya, S., Owaki, T., Morishima, N., Fukai, F., Mizuguchi, J., & Yoshimoto, T. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3871 · Cited by 222
STAT3 orchestrates contradictory signals in cytokine-induced G1 to S cell-cycle transition
Fukada, T., Ohtani, T., Yoshida, Y., Shirogane, T., Nishida, K., Nakajima, K., Hibi, M., & Hirano, T. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6670 · Cited by 247
Series Introduction: JAK-STAT signaling in human disease
Schindler, C. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15644 · Cited by 220
Self-citation
The Chemokine Monocyte Chemotactic Protein 1 Triggers Janus Kinase 2 Activation and Tyrosine Phosphorylation of the CCR2B Receptor
Mellado, M., Rodrı́guez-Frade, J. M., Aragay, A. M., del Real, G., Martín, Á., Vila‐Coro, A. J., Serrano, A., Mayor, F., & Martínez‐A, C. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.2.805 · Cited by 221
“Furthermore, STAT3, but not STAT5, is associated to the CCR2 following MCP-1 activation in accordance with the role assigned to the JAK tyrosine kinases in transducing signals from hemopoietic growth factor receptors (38).”
Background
IL-3 signaling and the role of Src kinases, JAKs and STATs: a covert liaison unveiled
Reddy, E. P., Korapati, A. L., Chaturvedi, P., & Rane, S. G. (2000) · Oncogene · doi:10.1038/sj.onc.1203594 · Cited by 224
“…of hematopoietic cells appears to result predominantly in the activation of JAK-2, although JAK-1 and TYK-2 have also been found to be activated in certain cell systems (Silvennoinen et al., 1993; Quelle et al., 1994; Lutticken et al., 1994; Chaturvedi et al., 1997, 1998; Jaster et al., 1997).”
Background
Interleukin 6 and liver regeneration
STREETZ, K. L., LUEDDE, T., MANNS, M. P., & TRAUTWEIN, C. (2000) · Gut · doi:10.1136/gut.47.2.309 · Cited by 238
SHP2 and SOCS3 Contribute to Tyr-759-dependent Attenuation of Interleukin-6 Signaling through gp130
Lehmann, U., Schmitz, J., Weissenbach, M., Sobota, R. M., Hörtner, M., Friederichs, K., Behrmann, I., Tsiaris, W., Sasaki, A., Schneider-Mergener, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210552200 · Cited by 236
Self-citation
Transcriptional regulation by the helix bundle peptide hormones: growth hormone, prolactin, and hematopoietic cytokines.
Horseman, N., & Yu-Lee, L. (1994) · Endocrine reviews · doi:10.1210/edrv-15-5-627 · Cited by 234
Leukemia Inhibitory Factor–dependent Transcriptional Activation in Embryonic Stem Cells
Bœuf, H., Hauss, C., Graeve, F. D., Baran, N., & Kédinger, C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.6.1207 · Cited by 231
“Activation of these kinases occurs as a result of LIFinduced dimerization of the receptor components (gp130LIFR b ) and leads to their phosphorylation (22, 31, 34, 52, 53).”
BackgroundInfluential
STAT3 antisense oligonucleotide AZD9150 in a subset of patients with heavily pretreated lymphoma: results of a phase 1b trial
Reilley, M. J., McCoon, P., Cook, C., Lyne, P., Kurzrock, R., Kim, Y., Woessner, R., Younes, A., Nemunaitis, J., Fowler, N., et al. (2018) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-018-0436-5 · Cited by 245
Targeting the Cytoplasmic and Nuclear Functions of Signal Transducers and Activators of Transcription 3 for Cancer Therapy
Germain, D., & Frank, D. A. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2491 · Cited by 221
The Lipopolysaccharide-Binding Protein Is a Secretory Class 1 Acute-Phase Protein Whose Gene Is Transcriptionally Activated by APRF/STAT-3 and Other Cytokine-Inducible Nuclear Proteins
Schumann, R. R., Kirschning, C. J., Unbehaun, A., Aberle, H., Knopf, H. P., Lamping, N., Ulevitch, R. J., & Herrmann, F. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3490 · Cited by 219
“This site is found in all acute-phase promoters, and our data agree with those of other studies, stressing the role of this site for IL-6-mediated gene activation (11, 12, 36).”
BackgroundResult
The Janus Protein Tyrosine Kinase Family and Its Role in Cytokine Signaling
Ihle, J. N. (1995) · Advances in immunology · doi:10.1016/s0065-2776(08)60582-9 · Cited by 210
STAT3 is constitutively activated in Hodgkin cell lines
Kube, D., Holtick, U., Vockerodt, M., Ahmadi, T., Haier, B., Behrmann, I., Heinrich, P. C., Diehl, V., & Tesch, H. (2001) · Blood · doi:10.1182/blood.v98.3.762 · Cited by 218
Self-citation
Protein Kinase C δ Associates with and Phosphorylates Stat3 in an Interleukin-6-dependent Manner
Jain, N. K., Zhang, T., Kee, W. H., Li, W., & Cao, X. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24392 · Cited by 206

Authors: Lütticken, C., Wegenka, U. M., Yuan, J., Buschmann, J., Schindler, C., Ziemiecki, A., Harpur, A. G., Wilks, A. F., Yasukawa, K., Taga, T., Kishimoto, T., Barbieri, G., Pellegrini, S., Sendtner, M., Heinrich, P. C., & Horn, F.
Affiliations: RWTH Aachen University (DE)
ORCID: Yuan, Juping
Wilks, Andrew F.
Yasukawa, Kiyoshi
Taga, Tetsuya
Kishimoto, Tadamitsu
Barbieri, Giovanna
Pellegrini, Sandra
Sendtner, Michael
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-01-07
Volume: 263
Issue: 5143
Pages: 89-92
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8272872
OpenAlex: W1999028040
Cited by: 814
References: 0
Citations by year: 2026: 4 · 2025: 8 · 2024: 11 · 2023: 5 · 2022: 7 · 2021: 13 · 2020: 10 · 2019: 14 · 2018: 14 · 2017: 17 · 2016: 17 · 2015: 23 · 2014: 15 · 2013: 15 · 2012: 20
FWCI: 38.85
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
RWTH Publications (RWTH Aachen) (submittedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Keywords: JAK1, gp130, IL-6 signaling, cytokine-receptor complex, tyrosine phosphorylation, transcription factor activation, leukemia inhibitory factor, oncostatin M, interleukin-11, ciliary neurotrophic factor, signal transduction
MeSH terms: Base Sequence, DNA-Binding Proteins, Humans, Interferon-gamma, Membrane Glycoproteins, Molecular Sequence Data, Phosphorylation, Protein-Tyrosine Kinases, Transcription Factors, Tumor Cells, Cultured, Tyrosine, Signal Transduction, Trans-Activators, Antigens, CD, Interleukin-6, Cytokines, STAT1 Transcription Factor, STAT3 Transcription Factor, Cytokine Receptor gp130, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit, Janus Kinase 1

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Association of Transcription Factor APRF and Protein Kinase Jak1 with the Interleukin-6 Signal Transducer gp130

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks