SOCS3 Exerts Its Inhibitory Function on Interleukin-6 Signal Transduction through the SHP2 Recruitment Site of gp130
Open accessAbstract
Interleukin-6 is involved in the regulation of many biological activities such as gene expression, cell proliferation, and differentiation. The control of the termination of cytokine signaling is as important as the regulation of initiation of signal transduction pathways. Three families of proteins involved in the down-regulation of cytokine signaling have been described recently: (i) SH2 domain-containing protein-tyrosine phosphatases (SHP), (ii) suppressors of cytokine signaling (SOCS), and (iii) protein inhibitors of activated STATs (PIAS). We have analyzed the interplay of two inhibitors in the signal transduction pathway of interleukin-6 and demonstrate that the tyrosine phosphatase SHP2 and SOCS3 do not act independently but are functionally linked. The activation of one inhibitor modulates the activity of the other; Inhibition of SHP2 activation leads to increased SOCS3-mRNA levels, whereas increased expression of SOCS3 results in a reduction of SHP2 phosphorylation after activation of the interleukin-6 signal transduction pathway. Furthermore, we show that tyrosine 759 in gp130 is essential for both SHP2 and SOCS3 but not for SOCS1 to exert their inhibitory activities on interleukin-6 signal transduction. Besides SHP2, SOCS3 also interacts with the Tyr(P)-759 peptide of gp130. Taken together, our results suggest differences in the function of SOCS1 and SOCS3 and a link between SHP2 and SOCS3.
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Inhibition of SOCS3 expression or lack of SOCS3 binding sites in gp130 results in sustained STAT3 activation and altered physiological outcomes in response to IL-6.
“Inhibition of SOCS3 expression [37] or lack of SOCS3 binding sites in gp130 results in sustained STAT3 activation and altered physiological outcomes in response to IL-6 [38].”
From The tyrosine phosphatase SHP2 increases robustness and information transfer within IL-6-induced JAK/STAT signalling (2021) · cites this paper as [38]
The introductory passage (page unavailable) says mutation of gp130 Tyr-759 produces enhanced and prolonged STAT3 activation and increased gene induction. The SOCS3-binding discussion (page unavailable) also reports that this mutation impairs SOCS3 inhibition of STAT3 and an acute-phase protein gene promoter. These passages support the signaling and gene-expression findings, but do not establish altered physiological outcomes. (LLM, conf=0.86)
Experimental — accuracy not yet measuredNascent SOCS-3 blocks the activation of STAT-3 by binding to the receptor complex via gp130 at tyrosine 759 and/or by binding and inhibiting Jak2 activity.
“In the first mechanism, nascent SOCS-3 blocks the activation of STAT-3 by binding to the receptor complex via gp130 at tyrosine 759 (34,35) and/or by binding and inhibiting Jak2 activity (36).”
From Expression of suppressors of cytokine signaling during liver regeneration (2001) · cites this paper as [34]
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Cites
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
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 · see citing works
Self-citationZhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070 · see citing works
A family of cytokine-inducible inhibitors of signalling
Starr, R., Willson, T. A., Viney, E. M., Murray, L. J. L., Rayner, J. R., Jenkins, B. J., Gonda, T. J., Alexander, W. S., Metcalf, D., Nicola, N. A., et al. (1997) · Nature · doi:10.1038/43206 · Cited by 2,066 · see citing works
A new protein containing an SH2 domain that inhibits JAK kinases
Endo, T. A., Masuhara, M., Yokouchi, M., Suzuki, R., Sakamoto, H., Mitsui, K., Matsumoto, A., Tanimura, S., Ohtsubo, M., Misawa, H., et al. (1997) · Nature · doi:10.1038/43213 · Cited by 1,408 · see citing works
Structure and function of a new STAT-induced STAT inhibitor
Naka, T., Narazaki, M., Hirata, M., Matsumoto, T., Minamoto, S., Aono, A., Nishimoto, N., Kajita, T., Taga, T., Yoshizaki, K., et al. (1997) · Nature · doi:10.1038/43219 · Cited by 1,287 · see citing works
Specific Inhibition of Stat3 Signal Transduction by PIAS3
Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980 · see citing works
Stahl, N., Farruggella, T. J., Boulton, T. G., Zhong, Z., Darnell, J. E., & Yancopoulos, G. D. (1995) · Science · doi:10.1126/science.7871433 · Cited by 979 · see citing works
Association and Activation of Jak-Tyk Kinases by CNTF-LIF-OSM-IL-6 β Receptor Components
Stahl, N., Boulton, T. G., Farruggella, T., Ip, N. Y., Davis, S., Witthuhn, B. A., Quelle, F. W., Silvennoinen, O., Barbieri, G., Pellegrini, S., et al. (1994) · Science · doi:10.1126/science.8272873 · Cited by 979 · see citing works
Lütticken, C., Wegenka, U. M., Yuan, J., Buschmann, J., Schindler, C., Ziemiecki, A., Harpur, A. G., Wilks, A. F., Yasukawa, K., Taga, T., et al. (1994) · Science · doi:10.1126/science.8272872 · Cited by 814 · see citing works
Self-citationInhibition of Stat1-mediated gene activation by PIAS1
Liu, B., Liao, J., Rao, X., Kushner, S. A., Chung, C. D., Chang, D. D., & Shuai, K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10626 · Cited by 765 · see citing works
Yasukawa, H., Misawa, H., Sakamoto, H., Masuhara, M., Sasaki, A., Wakioka, T., Ohtsuka, S., Imaizumi, T., Matsuda, T., Ihle, J. N., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1309 · Cited by 719 · see citing works
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 · see citing works
Murakami, M., Narazaki, M., Hibi, M., Yawata, H., Yasukawa, K., Hamaguchi, M., Taga, T., & Kishimoto, T. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11349 · Cited by 589 · see citing works
Wegenka, U. M., Buschmann, J., Lütticken, C., Heinrich, P. C., & Horn, F. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.276 · Cited by 553 · see citing works
Self-citationActivation of a Phosphotyrosine Phosphatase by Tyrosine Phosphorylation
Vogel, W. F., Lammers, R., Huang, J., & Ullrich, A. (1993) · Science · doi:10.1126/science.7681217 · Cited by 549 · see citing works
Guschin, D. Y., Rogers, N. C., Briscoe, J., Witthuhn, B. A., Watling, D., Horn, F., Pellegrini, S., Yasukawa, K., Heinrich, P. C., & Stark, G. R. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07128.x · Cited by 434 · see citing works
Self-citationContribution of STAT SH2 Groups to Specific Interferon Signaling by the Jak-STAT pathway
Heim, M. H., Kerr, L. M., Stark, G. R., & Darnell, J. E., Jr. (1995) · Science · doi:10.1126/science.7871432 · Cited by 425 · see citing works
Regulation of Interferon-γ-Activated STAT1 by the Ubiquitin-Proteasome Pathway
Kim, T. K., & Maniatis, T. (1996) · Science · doi:10.1126/science.273.5282.1717 · Cited by 410 · see citing works
Nicholson, S. E., Willson, T. A., Farley, A., Starr, R., Zhang, J., Baca, M., Alexander, W. S., Metcalf, D., Hilton, D. J., & Nicola, N. A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.2.375 · Cited by 407 · see citing works
Sasaki, A., Yasukawa, H., Suzuki, A., Kamizono, S., Syoda, T., Kinjyo, I., Sasaki, M., Johnston, J. A., & Yoshimura, A. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00263.x · Cited by 398 · see citing works
Gerhartz, C., Heesel, B., Sasse, J., Hemmann, U., Landgraf, C., Schneider-Mergener, J., Horn, F., Heinrich, P., & Graeve, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12991 · Cited by 351 · see citing works
Self-citationHaspel, R. L., Salditt‐Georgieff, M., & Darnell, J. E. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01016.x · Cited by 312 · see citing works
Sengupta, T. K., Talbot, E. S., Scherle, P., & Ivashkiv, L. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.19.11107 · Cited by 245 · see citing works
Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK)
Jain, N., Zhang, T., Fong, S., Lim, C. P., & Cao, X. (1998) · Oncogene · doi:10.1038/sj.onc.1202238 · Cited by 213 · see citing works
Hemmann, U., Gerhartz, C., Heesel, B., Sasse, J., Kurapkat, G., Grötzinger, J., Wollmer, A., Zhong, Z., Darnell, J., Graeve, L., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12999 · Cited by 197 · see citing works
Self-citationYuan, J., Wegenka, U. M., Lütticken, C., Buschmann, J., Decker, T., Schindler, C., Heinrich, P. C., & Horn, F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1657 · Cited by 179 · see citing works
Self-citationSCHAPER, F., GENDO, C., ECK, M., SCHMITZ, J., GRIMM, C., ANHUF, D., KERR, I. M., & HEINRICH, P. C. (1998) · Biochemical Journal · doi:10.1042/bj3350557 · Cited by 178 · see citing works
Self-citationArcone, R., Pucci, P., Zappacosta, F., Fontaine, V., Malorni, A., Marino, G., & Ciliberto, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16048.x · Cited by 136 · see citing works
Symes, A., Stahl, N., Reeves, S. A., Farruggella, T., Servidei, T., Gearan, T., Yancopouloš, G., & Fink, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00298-3 · Cited by 133 · see citing works
Kim, H., Hawley, T. S., Hawley, R. G., & Baumann, H. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1525 · Cited by 119 · see citing works
Soluble human interleukin-6 receptor. Expression in insect cells, purification and characterization.
Weiergräber, O., Hemmann, U., Küster, A., Müller-Newen, G., Schneider, J., Rose-John, S., Kurschat, P., Brakenhoff, J., Hart, M. H. L., Stabel, S., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.661_b.x · Cited by 101 · see citing works
Self-citationSuzuki, R., Sakamoto, H., Yasukawa, H., Masuhara, M., Wakioka, T., Sasaki, A. T., Yuge, K., Komiya, S., Inoue, A., & Yoshimura, A. (1998) · Oncogene · doi:10.1038/sj.onc.1202143 · Cited by 88 · see citing works
Horsten, U., Müller-Newen, G., Gerhartz, C., Wollmer, A., Wijdenes, J., Heinrich, P., & Grötzinger, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23748 · Cited by 76 · see citing works
Self-citationTerstegen, L., Gatsios, P., Bode, J. G., Schaper, F., Heinrich, P. C., & Graeve, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m904148199 · Cited by 74 · see citing works
Self-citationGatsios, P., Haubeck, H., van de Leur, E., Frisch, W., Apte, S., Greiling, H., Heinrich, P., & Graeve, L. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0056t.x · Cited by 68 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 4
- Liu, B., Liao, J. Y., Rao, X. P., Kushner, S. A., Chung, C. D., Chang, D. D., and Shuai, K. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 10626 -10631
- Murakami, M., Narazaki, M., Hibi, M., Yawata, H., Yasukawa, K., Hamaguchi, M., Taga, T., and Kishimoto, T. (1991) Proc. Natl. Acad. Sci.
- Sengupta, T. K., Talbot, E. S., Scherle, P. A., and Ivashkiv, L. B. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 11107-11112
- Terstegen, L., Gatsios, P., Bode, J. G., Schaper, F., Heinrich, P. C., and Graeve, L. (2000) J. Biol. Chem. 275, in press
Cited by
Sorted by citations
IL‐6 in inflammation, immunity, and disease
Tanaka, T., Narazaki, M., & Kishimoto, T. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016295 · Cited by 5,046 · see citing works
“In this context, SOCS1 binds to tyrosine-phosphorylated JAK (Naka et al. 1997), whereas SOCS3 binds to tyrosine-phosphorylated gp130 (Schmitz et al. 2000) to stop IL-6 signaling by means of a negative feedback loop.”
BackgroundPrinciples 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 · see citing works
Self-citationYing, Q.-L., Nichols, J., Chambers, I., & Smith, A. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00847-x · Cited by 2,114 · see citing works
“…(Schorpp-Kistner et al.,stimulated with LIF plus BMP. Immunoprecipation fol- lowing transfection with FLAG-tagged Smad1 indicated 1999), and SOCS3 functions as a negative feedback regulator of gp130 signaling (Schmitz et al., 2000) thatthat activated STAT3 and Smad1 may colocalize (Figure 3F).”
IL-6 in inflammation, autoimmunity and cancer
Hirano, T. (2021) · International Immunology · doi:10.1093/intimm/dxaa078 · Cited by 1,453 · see citing works
“SOCS3 is induced by STAT3 and considered to regulate a major negative feedback loop of a gp130-mediated signaling pathway (118–120).”
BackgroundThe ‘Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
Neel, B. G., Gu, H., & Pao, L. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00091-4 · Cited by 1,249 · see citing works
The JAK-STAT Signaling Pathway: Input and Output Integration
Murray, P. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.2623 · Cited by 1,179 · see citing works
Signaling through the JAK/STAT pathway, recent advances and future challenges
Kisseleva, T., Bhattacharya, S., Braunstein, J., & Schindler, C. (2002) · Gene · doi:10.1016/s0378-1119(02)00398-0 · Cited by 1,158 · see citing works
The molecular details of cytokine signaling via the JAK/STAT pathway
Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 865 · see citing works
SOCS Proteins: Negative Regulators of Cytokine Signaling
Krebs, D. L., & Hilton, D. J. (2001) · Stem Cells · doi:10.1634/stemcells.19-5-378 · Cited by 826 · see citing works
Regulation of cytokine signaling and inflammation
Hanada, T., & Yoshimura, A. (2002) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00026-6 · Cited by 748 · see citing works
Signalling, cell cycle and pluripotency in embryonic stem cells
Burdon, T., Smith, A. T., & Savatier, P. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02352-8 · Cited by 710 · see citing works
The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response.
Alexander, W., & Hilton, D. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.091003.090312 · Cited by 774 · see citing works
Suppressors of cytokine signalling (SOCS) in the immune system
Alexander, W. S. (2002) · Nature reviews. Immunology · doi:10.1038/nri818 · Cited by 645 · see citing works
Senn, J. J., Klover, P. J., Nowak, I. A., Zimmers, T. A., Koniaris, L. G., Furlanetto, R. W., & Mooney, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210689200 · Cited by 620 · see citing works
Shaping Gene Expression in Activated and Resting Primary Macrophages by IL-10
Lang, R., Patel, D. H., Morris, J. J., Rutschman, R. L., & Murray, P. J. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.5.2253 · Cited by 613 · see citing works
“SOCS3 binds to gp130 (37, 38), the signaling component of IL-6 family cytokine receptors (39), but may have additional targets, as overexpression studies have shown that it can inhibit”
BackgroundSOCS3, a Major Regulator of Infection and Inflammation
Carow, B., & Rottenberg, M. E. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00058 · Cited by 555 · see citing works
SOCS3 Mediates Feedback Inhibition of the Leptin Receptor via Tyr985
Bjørbæk, C., Lavery, H. J., Bates, S. H., Olson, R. K., Davis, S. M., Flier, J. S., & Myers, M. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007577200 · Cited by 537 · see citing works
Pleiotropy and specificity: insights from the interleukin 6 family of cytokines
Murakami, M., Kamimura, D., & Hirano, T. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.027 · Cited by 533 · see citing works
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 511 · see citing works
“Also SOCS3 binds to the phosphotyrosine motif 759 within gp130 to inhibit IL-6 signaling [92,93].”
BackgroundSelf-citationThe paradigm of IL-6: from basic science to medicine.
Naka, T., Nishimoto, N., & Kishimoto, T. (2002) · Arthritis Research · doi:10.1186/ar565 · Cited by 480 · see citing works
Leukemia inhibitory factor (LIF)
Nicola, N. A., & Babon, J. J. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.07.001 · Cited by 478 · see citing works
“Interestingly, the site on gp130 (and potentially LIFRβ) to which SOCS3 binds is the phosphotyrosine motif that usually recruits SHP2 (also known as PTNP11) to activate the MAP-kinase pathway (see below) [53].”
BackgroundTebbutt, N. C., Giraud, A. S., Inglese, M., Jenkins, B., Waring, P., Clay, F. J., Malki, S., Alderman, B. M., Grail, D., Hollande, F., et al. (2002) · Nature Medicine · doi:10.1038/nm763 · Cited by 474 · see citing works
“Similarly, enhanced STAT3 activation in gp130 757F mice is likely to result from impaired SOCS-3 binding to the mutated 757F residu”
BackgroundInhibitors of Cytokine Signal Transduction
Wormald, S., & Hilton, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r300030200 · Cited by 440 · see citing works
SOCS3 regulates the plasticity of gp130 signaling
Lang, R., Pauleau, A.-L., Parganas, E., Takahashi, Y., Mages, J., Ihle, J. N., Rutschman, R., & Murray, P. J. (2003) · Nature Immunology · doi:10.1038/ni932 · Cited by 439 · see citing works
“SOCS3 probably binds phosphorylated gp130 and regulates the subsequent activation of STAT3 (refs”
BackgroundUnderstanding and exploiting the endogenous interleukin-10/STAT3-mediated anti-inflammatory response
MURRAY, P. (2006) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2006.01.010 · Cited by 436 · see citing works
The SOCS box: a tale of destruction and degradation
Kile, B. T., Schulman, B. A., Alexander, W. S., Nicola, N. A., Martin, H. M., & Hilton, D. J. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02085-6 · Cited by 433 · see citing works
Interleukin (IL-6) ImmunotherapyPreprint
Tanaka, T., Narazaki, M., & Kishimoto, T. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028456 · Cited by 407 · see citing works
“STAT3 also induces the suppressor of cytokine signaling (SOCS)1 and SOCS3, which bind to tyrosine-phosphorylated JAK (Naka et al. 1997) and tyrosine-phosphorylated gp130 (Schmitz et al. 2000), respectively, to stop IL-6 signaling by means of a negative feedback loop.”
BackgroundPlasticity and cross-talk of Interleukin 6-type cytokines
Garbers, C., Hermanns, H. M., Schaper, F., Müller‐Newen, G., Grötzinger, J., Rose‐John, S., & Scheller, J. (2012) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2012.04.001 · Cited by 401 · see citing works
Self-citationShouda, T., Yoshida, T., Hanada, T., Wakioka, T., Oishi, M., Miyoshi, K., Komiya, S., Kosai, K.-I., Hanakawa, Y., Hashimoto, K., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13568 · Cited by 394 · see citing works
Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors
Bjørbæk, C., Buchholz, R. M., Davis, S. M., Bates, S. H., Pierroz, D. D., Gu, H., Neel, B. G., Myers, M. G., & Flier, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007439200 · Cited by 364 · see citing works
CIS3/SOCS-3 Suppresses Erythropoietin (EPO) Signaling by Binding the EPO Receptor and JAK2
Sasaki, A. T., Yasukawa, H., Shouda, T., Kitamura, T., Đikić, I., & Yoshimura, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003456200 · Cited by 341 · see citing works
Interleukin 10 Receptor Signaling
Shouval, D. S., Ouahed, J., Biswas, A., Goettel, J. A., Horwitz, B. H., Klein, C., Muise, A. M., & Snapper, S. B. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800267-4.00005-5 · Cited by 307 · see citing works
Acquiring signalling specificity from the cytokine receptor gp130
Ernst, M. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.003 · Cited by 297 · see citing works
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 · see citing works
“The gp130 peptides comprising pY759 and pY915 behaved as previously described (26).”
BackgroundInfluentialSelf-citationSOCS3 Is a Critical Physiological Negative Regulator of G-CSF Signaling and Emergency Granulopoiesis
Croker, B. A., Metcalf, D., Robb, L., Wei, W., Mifsud, S., DiRago, L., Cluse, L. A., Sutherland, K. D., Hartley, L., Williams, E., et al. (2004) · Immunity · doi:10.1016/s1074-7613(04)00022-6 · Cited by 285 · see citing works
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 · see citing works
Berlato, C., Cassatella, M. A., Kinjyo, I., Gatto, L., Yoshimura, A., & Bazzoni, F. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.12.6404 · Cited by 267 · see citing works
Oncostatin M and interleukin-31: Cytokines, receptors, signal transduction and physiology
Hermanns, H. M. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.07.006 · Cited by 263 · see citing works
“ment site for SOCS proteins similar to what has been shown for gp130 is unclear [146].”
BackgroundSOCS2 negatively regulates growth hormone action in vitro and in vivo
Greenhalgh, C. J., Rico-Bautista, E., Lorentzon, M., Thaus, A. L., Morgan, P. O., Willson, T. A., Zervoudakis, P., Metcalf, D., Street, I. P., Nicola, N. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci200522710 · Cited by 257 · see citing works
Kontoyiannis, D. L., Kotlyarov, A., Carballo, E., Alexopoulou, L., Blackshear, P. J., Gaestel, M., Davis, R. J., Flavell, R. A., & Kollias, G. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.14.3760 · Cited by 255 · see citing works
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 252 · see citing works
“1) [33, 35, 36].”
BackgroundSOCS, Inflammation, and Autoimmunity
Yoshimura, A., Suzuki, M., Sakaguchi, R., Hanada, T., & Yasukawa, H. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00020 · Cited by 254 · see citing works
“SOCS3 binds to gp130-related cytokine receptors, including the phosphorylated tyrosine 757 (Tyr757) residue of gp130, the Tyr800 residue of IL-12 receptor β2, and Tyr985 of the leptin receptor (Bjorbak et al., 2000; Sasaki et al., 2000; Schmitz et al., 2000; Lehmann et al., 2003; Yamamoto et al., 2003).”
BackgroundJAK/STAT signal transduction: Regulators and implication in hematological malignancies
Valentino, L., & Pierre, J. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.12.017 · Cited by 252 · see citing works
Placental defects and embryonic lethality in mice lacking suppressor of cytokine signaling 3
Roberts, A. W., Robb, L., Rakar, S., Hartley, L., Cluse, L., Nicola, N. A., Metcalf, D., Hilton, D. J., & Alexander, W. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161271798 · Cited by 300 · see citing works
Activation of STAT3 by the Hepatitis C Virus Core Protein Leads to Cellular Transformation
Yoshida, T., Hanada, T., Tokuhisa, T., Kosai, K.-I., Sata, M., Kohara, M., & Yoshimura, A. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20012127 · Cited by 236 · see citing works
“On the other hand, SOCS3 binds to gp130 as well as to JAKs and inhibits JAK tyrosine kinase activity (30, 31).”
BackgroundStat3 Activation Is Limiting for Reprogramming to Ground State Pluripotency
Yang, J. P., van Oosten, A. L., Theunissen, T. W., Guo, G., Silva, J., & Smith, A. G. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.06.022 · Cited by 232 · see citing works
“Furthermore, because tyrosine 118 is also the binding site for the negative feedback regulator Socs3 (Schmitz et al., 2000), GY118F induces elevated and sustained activation of Jak/Stat3 (Burdon et al.”
BackgroundSHP2 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 · see citing works
Self-citationCellular and Oxidative Mechanisms Associated with Interleukin-6 Signaling in the Vasculature
Didion, S. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122563 · Cited by 235 · see citing works
Regulation of cytokine signaling by SOCS family molecules
Fujimoto, M., & Naka, T. (2003) · Trends in Immunology · doi:10.1016/j.it.2003.10.008 · Cited by 228 · see citing works
General nature of the STAT3-activated anti-inflammatory response.
El Kasmi, K. C., Holst, J., Coffre, M., Mielke, L., de Pauw, A., Lhocine, N., Smith, A. M., Rutschman, R., Kaushal, D., Shen, Y., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7880 · Cited by 225 · see citing works
Atsumi, T., Ishihara, K., Kamimura, D., Ikushima, H., Ohtani, T., Hirota, S., Kobayashi, H., Park, S.-J., Saeki, Y., Kitamura, Y., et al. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020619 · Cited by 225 · see citing works
“Transcription levels of SOCS-3 mRNA were estimated by quantitative RT-PCR.”
BackgroundInfluentialSustained IL-6/STAT-3 Signaling in Cholangiocarcinoma Cells Due to SOCS-3 Epigenetic Silencing
Isomoto, H., Mott, J. L., Kobayashi, S., Werneburg, N. W., Bronk, S. F., Haan, S., & Gores, G. J. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.10.037 · Cited by 219 · see citing works
“23, 25, 27, 28 By binding to this residue, SOCS-3 is able to inhibit IL-6 signaling thereby turning it off in a classic feed back loop.”
BackgroundSelf-citationSuppressors of cytokine signalling: SOCS
Larsen, L., & Röpke, C. (2002) · Apmis · doi:10.1034/j.1600-0463.2002.1101201.x · Cited by 219 · see citing works
“Mutating this residue (Y759) impairs the inhibitory action of SOCS-3 on both STAT1 and STAT3 and gene promotor induction (30, 31).”
BackgroundInhibition of IL-6 family cytokines by SOCS3
Babon, J. J., Varghese, L. N., & Nicola, N. A. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2013.12.004 · Cited by 214 · see citing works
“The interaction between the SOCS3 SH2 domain and gp130 has been well described both biochemically[56, 57, 59] and structurally[61] (see Figure 2b) and there are a number of features of the interaction responsible for its high affinity that are worth noting.”
BackgroundDesign and application of a cytokine-receptor-based interaction trap
Eyckerman, S., Verhee, A., der Heyden, J. V., Lemmens, I. H., Ostade, X. V., Vandekerckhove, J. S., & Tavernier, J. H. (2001) · Nature Cell Biology · doi:10.1038/ncb1201-1114 · Cited by 209 · see citing works
Signaling by Type I and II cytokine receptors: ten years after
Gadina, M., Hilton, D. J., Johnston, J. A., Morinobu, A., Lighvani, A., Zhou, Y., Visconti, R., & O’Shea, J. J. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00228-4 · Cited by 206 · see citing works
The SH2 domain: versatile signaling module and pharmaceutical target.
Machida, K., & Mayer, B. (2005) · Biochimica et Biophysica Acta · doi:10.1016/j.bbapap.2004.10.005 · Cited by 218 · see citing works
Bourillot, P.-Y., Aksoy, I., Schreiber, V., Wianny, F., Schulz, H., Hummel, O., Hübner, N., & Savatier, P. (2009) · Stem Cells · doi:10.1002/stem.110 · Cited by 202 · see citing works
“above-mentioned genes, Socs3, which encodes the suppressor of cytokine signaling 3 (SOCS3), functions as a feedback regulator of gp130 signaling [ 12 ] that blocks self-renewal when overexpressed [2].”
Linard, C., Marquette, C., Mathieu, J., Pennequin, A., Clarençon, D., & Mathé, D. (2004) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2003.09.039 · Cited by 189 · see citing works
Regulation of innate immunity by suppressor of cytokine signaling (SOCS) proteins
Dalpke, A. H., Heeg, K. M., Bartz, H., & Baetz, A. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.10.008 · Cited by 184 · see citing works
Ogata, H., Kobayashi, T., Chinen, T., Takaki, H., Sanada, T., Minoda, Y., Koga, K., Takaesu, G., Maehara, Y., Iida, M., et al. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.04.025 · Cited by 183 · see citing works
IL-6, IL-17 and STAT3: a holy trinity in auto-immunity?
Camporeale, A. (2012) · Frontiers in bioscience · doi:10.2741/4054 · Cited by 175 · see citing works
“Finally, SOCS3, a STAT3 immediate early target gene, is recruited to the same phosphotyrosine residue as SHP2, mediating a negative feedback via inactivation of JAKs (23).”
BackgroundInterleukin-6 signalling: More than Jaks and STATs
Eulenfeld, R., Dittrich, A., Khouri, C., Müller, P. J., Mütze, B., Wolf, A., & Schaper, F. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.010 · Cited by 171 · see citing works
Self-citationA new era for the treatment of inflammatory autoimmune diseases by interleukin-6 blockade strategy
Tanaka, T., Narazaki, M., Ogata, A., & Kishimoto, T. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.01.009 · Cited by 166 · see citing works
Expression of suppressors of cytokine signaling during liver regeneration
Campbell, J. S., Prichard, L., Schaper, F., Schmitz, J., Stephenson-Famy, A., Rosenfeld, M. E., Argast, G. M., Heinrich, P. C., & Fausto, N. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11867 · Cited by 156 · see citing works
“In the first mechanism, nascent SOCS-3 blocks the activation of STAT-3 by binding to the receptor complex via gp130 at tyrosine 759 (34, 35) and/or by binding and inhibiting Jak2 activity (36).”
BackgroundSelf-citationSands, W. A., Woolson, H. D., Milne, G. R., Rutherford, C. L., & Palmer, T. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00207-06 · Cited by 156 · see citing works
“SOCS-3 can also potentially competitively block receptor recruitment of SHP-2 to Tyr759 of gp130, thus inhibiting ERK activation (43).”
BackgroundDunn, S. L., Björnholm, M., Bates, S., Chen, Z., Seifert, M. M., & Myers, M. G. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0353 · Cited by 169 · see citing works
Brocke-Heidrich, K., Kretzschmar, A., Pfeifer, G., Henze, C., Löffler, D., Koczan, D., Thiesen, H., Burger, R., Gramatzki, M., & Horn, F. (2004) · Blood · doi:10.1182/blood-2003-04-1048 · Cited by 166 · see citing works
“The JAKs phosphorylate gp130 tyrosine residues which then serve as docking sites for src homology 2 (SH2) domain-containing signaling molecules such as the signal transducers and activators of transcription 3 and 1 (Stat3, Stat1),(3,4) the SH2-containing phosphatase-2 (SHP-2), and the suppressor of cytokine signaling-…”
BackgroundNarimatsu, M., Maeda, H., Itoh, S., Atsumi, T., Ohtani, T., Nishida, K., Itoh, M., Kamimura, D., Park, S., Mizuno, K., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6615-6625.2001 · Cited by 145 · see citing works
“YSTV motif in gp130, causing negative feedback (27, 34).”
BackgroundIdentification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor
Eyckerman, S., Broekaert, D., Verhee, A., Vandekerckhove, J. S., & Tavernier, J. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02205-5 · Cited by 142 · see citing works
Inhibition of IL-6 and IL-10 Signaling and Stat Activation by Inflammatory and Stress Pathways
Ahmed, S. T., & Ivashkiv, L. B. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.9.5227 · Cited by 141 · see citing works
“Another key feature of the truncated receptor is that it lacks the Y759 SH2 domain-containing protein-tyrosine phosphatase/SOCS3 docking site (55, 56, 64), lending further support for the SOCSindependent nature of the inhibition seen in our system.”
BackgroundInfluentialThe role of the interleukin‐6 family of cytokines in inflammatory arthritis and bone turnover
Wong, P. K. K., Campbell, I. K., Egan, P. J., Ernst, M., & Wicks, I. P. (2003) · Arthritis & Rheumatism · doi:10.1002/art.10943 · Cited by 140 · see citing works
The Src Family of Tyrosine Kinases Is Important for Embryonic Stem Cell Self-renewal
Annerén, C., Cowan, C. A., & Melton, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403547200 · Cited by 140 · see citing works
Pernot, F., Heinrich, C., Barbier, L., Peinnequin, A., Carpentier, P., Dhote, F., Baille, V., Beaup, C., Depaulis, A., & Dorandeu, F. (2011) · Epilepsia · doi:10.1111/j.1528-1167.2011.03273.x · Cited by 134 · see citing works
“More precisely, SOCS3 is induced by a wide range of stimuli including interleukin-6 (IL-6) family and regulates the cytokine signaling via the inhibition of the Janus kinases/ signal transducers and activators of transcription (JAK/ STAT) transduction pathway in a negative feedback loop (Heinrich et al., 1998; Schmitz…”
BackgroundDominant-negative mutations in human IL6ST underlie hyper-IgE syndrome
Béziat, V., Tavernier, S. J., Chen, Y., Ma, C. S., Materna, M., Laurence, A. D. J., Staal, J., Aschenbrenner, D., Roels, L., Worley, L., et al. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20191804 · Cited by 134 · see citing works
“Upon phosphorylation, Y759 acts as a docking site for SOCS3, which switches off STAT3 activation (Nicholson et al., 2000; Schmitz et al., 2000).”
The role of the interleukin (IL)-6/IL-6 receptor axis in cancer.
Taher, M. Y., Davies, D., & Maher, J. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180136 · Cited by 115 · see citing works
Ivo, P. T. (2006) · Frontiers in bioscience · doi:10.2741/2103 · Cited by 130 · see citing works
“Because Tyr729 is also a docking site for the protein tyrosine phosphatase SHP-2, which binds to and inactivates STAT5, a model is suggested in which the loss of recruitment of both SOCS3 and SHP-2 to the activated receptor complex determine the increased STAT5/STAT3 activation ratio and the resulting signaling abnorm…”
BackgroundInfluentialKalliolias, G. D., & Ivashkiv, L. B. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.9.6325 · Cited by 132 · see citing works
Yamamoto, K., Yamaguchi, M., Miyasaka, N., & Miura, O. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.140 · Cited by 131 · see citing works
Hörtner, M., Nielsch, U., Mayr, L. M., Johnston, J. A., Heinrich, P. C., & Haan, S. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.3.1219 · Cited by 128 · see citing works
“We and others have recently reported that SOCS-3 exerts part of its inhibitory action on IL-6 signal transduction by binding to pY759 within the signal transducing receptor subunit gp130 (31, 32).”
Self-citationJiang, M., Chen, J., Zhang, W., Zhang, R., Ye, Y., Liu, P., Yu, W., Wei, F., Ren, X., & Yu, J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01840 · Cited by 127 · see citing works
Regulation of the immune system by SOCS family adaptor proteins
Ilangumaran, S., Ramanathan, S., & Rottapel, R. K. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.08.015 · Cited by 127 · see citing works
The biology and mechanism of action of Suppressor of Cytokine Signaling 3 (SOCS3)
Babon, J., & Nicola, N. (2012) · Growth Factors · doi:10.3109/08977194.2012.687375 · Cited by 121 · see citing works
“Of all other SH2 domains, only the SH2 domain of SHP-2 is similar in this regard and SHP-2 is known to target SOCS3 binding sites on several receptors (Nicholson et al. 2000; Schmitz et al. 2000; Fairlie et al. 2003).”
BackgroundProlonged inflammatory gene response following soman-induced seizures in mice
Dhote, F., Peinnequin, A., Carpentier, P., Baille, V., Delacour, C., Foquin, A., Lallement, G., & Dorandeu, F. (2007) · Toxicology · doi:10.1016/j.tox.2007.05.032 · Cited by 125 · see citing works
Jak-Stat Signaling Induced by Interleukin-6 Family Cytokines in Hepatocellular Carcinoma
Lokau, J., Schoeder, V., Haybaeck, J., & Garbers, C. (2019) · Cancers · doi:10.3390/cancers11111704 · Cited by 124 · see citing works
“Cancers 2019, 11, 1704 5 of 17 Cancers 2019, 11, 1704 5 of 17 Of note, SHP2 does not only act as negative regulator for STATs, but is also phosphorylated upon gp130 activation and subsequently, activates the PI3K and MAPK signaling cascades [43].”
BackgroundInfluentialMolecular basis of the cell specificity of cytokine action
Ishihara, K., & Hirano, T. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00321-x · Cited by 122 · see citing works
Emerging roles for the IL-6 family of cytokines in pancreatic cancer
van Duijneveldt, G., Griffin, M. D. W., & Putoczki, T. L. (2020) · Clinical Science · doi:10.1042/cs20191211 · Cited by 118 · see citing works
Chen, H., Ördög, T., Chen, J., Young, D. L., Bardsley, M. R., Redelman, D. D., Ward, S. M., & Sanders, K. M. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00113.2007 · Cited by 119 · see citing works
“Thus, in ICC, Socs3 may be involved not only in feedback regulation of IL-6 signaling but also in signaling from the other receptor tyrosine kinases expressed in these cells.”
BackgroundInfluentialTyrosine Phosphorylation Disrupts Elongin Interaction and Accelerates SOCS3 Degradation
Haan, S., FERGUSON, P. W., Sommer, U., Hiremath, M. M., McVicar, D. W., Heinrich, P. C., Johnston, J. A., & Cacalano, N. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303170200 · Cited by 119 · see citing works
Self-citationvan Oosten, A. L., Costa, Y., Smith, A. G., & Silva, J. (2012) · Nature Communications · doi:10.1038/ncomms1822 · Cited by 116 · see citing works
Ehlting, C., Lai, W. S., Schaper, F., Brenndörfer, E. D., Matthes, R.-J., Heinrich, P. C., Ludwig, S., Blackshear, P. J., Gaestel, M., Häussinger, D., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.2813 · Cited by 112 · see citing works
“E-mail address: Johannes.Bode@t-online.de 3 Abbreviations used in this paper: SOCS, suppressor of cytokine signaling; ARE, adenosine/uridine-rich element; CT, delta cycle threshold; DIG, digoxygenin; Epo, erythropoietin; HA, hemagglutinin; MEF, mouse embryonic fibroblast; MK2, MAPKactivated protein kinase 2; MKK6, MAP…”
BackgroundMethodInfluentialSelf-citationA Stat3-interacting protein (StIP1) regulates cytokine signal transduction.
Collum, R. G., Brutsaert, S., Lee, G., & Schindler, C. W. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.170192197 · Cited by 113 · see citing works
Cholinergic agonists regulate JAK2/STAT3 signaling to suppress endothelial cell activation
Chatterjee, P. K., Al‐Abed, Y., Sherry, B. A., & Metz, C. N. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00160.2009 · Cited by 111 · see citing works
“Based on previous reports revealing that 1) SHP2 phosphorylation is impaired by SOCS3 expression; 2) SOCS3 requires SHP2 recruitment site in gp130 to exerts its effect on acute phase proteins, and 3) SHP2 appears to exert part of its effect on the JAK/STAT3 pathway through the recruitment of SOCS3 to the receptor comp…”
BackgroundNerstedt, A., Johansson, A., Andersson, C. X., Cansby, E., Smith, U., & Mahlapuu, M. (2010) · Diabetologia · doi:10.1007/s00125-010-1856-z · Cited by 106 · see citing works
Qasimi, P., Ming‐Lum, A., Ghanipour, A., Ong, C. J., Cox, M., Ihle, J. N., Cacalano, N. A., Yoshimura, A., & Mui, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508608200 · Cited by 105 · see citing works
ADAM17 Activity and IL-6 Trans-Signaling in Inflammation and Cancer
Schumacher, N., & Rose‐John, S. (2019) · Cancers · doi:10.3390/cancers11111736 · Cited by 103 · see citing works
Hypothalamic Regulation of Corticotropin-Releasing Factor under Stress and Stress Resilience
Kageyama, K., Iwasaki, Y., & Daimon, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212242 · Cited by 104 · see citing works
Teramo, A., Gattazzo, C., Passeri, F., Liço, A., Tasca, G., Cabrelle, A., Martini, V., Frezzato, F., Trimarco, V., Ave, E., et al. (2013) · Blood · doi:10.1182/blood-2012-07-441378 · Cited by 104 · see citing works
Li, C., Iness, A. N., Yoon, J., Grider, J. R., Murthy, K. S., Kellum, J. M., & Kuemmerle, J. F. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401779 · Cited by 103 · see citing works
“more often associated with IL-6 signaling than SOCS2 (35, 36).”
InfluentialOberg, H., Wesch, D., Grüssel, S., Rose‐John, S., & Kabelitz, D. (2006) · International Immunology · doi:10.1093/intimm/dxh396 · Cited by 102 · see citing works
- Authors
- Schmitz, J., Weissenbach, M., Haan, S., Heinrich, P. C., & Schaper, F.
- Affiliations
- RWTH Aachen University (DE)
- Corresponding author
- Heinrich, Peter C.
- ORCID
- Schaper, Fred
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-04
- Volume
- 275
- Issue
- 17
- Pages
- 12848-12856
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038468714
- Cited by
- 388
- References
- 36
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 4 · 2023: 3 · 2022: 9 · 2021: 10 · 2020: 10 · 2019: 7 · 2018: 8 · 2017: 14 · 2016: 10 · 2015: 10 · 2014: 13 · 2013: 10 · 2012: 23
- FWCI
- 15.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, cc-by-nc-sa)
- RWTH Publications (RWTH Aachen) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- SOCS3, IL-6 signaling, SHP2, gp130, suppressor of cytokine signaling, SOCS1, protein-protein interaction
- MeSH terms
- Suppressor of Cytokine Signaling 1 Protein, Suppressor of Cytokine Signaling 3 Protein, Interleukin-6 Inhibitors, alpha-Macroglobulins, Carrier Proteins, Cell Nucleus, Glutathione Transferase, Humans, Membrane Glycoproteins, Phosphorylation, Precipitin Tests, Promoter Regions, Genetic, Protein Binding, Proteins, Recombinant Fusion Proteins, Repressor Proteins, Transcription Factors, Transfection, Tumor Cells, Cultured, Tyrosine, Immunoblotting, Blotting, Northern, Signal Transduction, Antigens, CD, Interleukin-6, Protein Tyrosine Phosphatases, src Homology Domains, Intracellular Signaling Peptides and Proteins, Cytokine Receptor gp130, Suppressor of Cytokine Signaling Proteins, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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