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Activation of the protein tyrosine phosphatase SHP2 via the interleukin-6 signal transducing receptor protein gp130 requires tyrosine kinase Jak1 and limits acute-phase protein expression
Open accessAbstract
Stimulation of the interleukin-6 (IL-6) signalling pathway occurs via the IL-6 receptor–glycoprotein 130 (IL-6R–gp130) receptor complex and results in the regulation of acute-phase protein genes in liver cells. Ligand binding to the receptor complex leads to tyrosine phosphorylation and activation of Janus kinases (Jak), phosphorylation of the signal transducing subunit gp130, followed by recruitment and phosphorylation of the signal transducer and activator of transcription factors STAT3 and STAT1 and the src homology domain (SH2)-containing protein tyrosine phosphatase (SHP2). The tyrosine phosphorylated STAT factors dissociate from the receptor, dimerize and translocate to the nucleus where they bind to enhancer sequences of IL-6 target genes. Phosphorylated SHP2 is able to bind growth factor receptor bound protein (grb2) and thus might link the Jak/STAT pathway to the ras/raf/mitogen-activated protein kinase pathway. Here we present data on the dose-dependence, kinetics and kinase requirements for SHP2 phosphorylation after the activation of the signal transducer, gp130, of the IL-6-type family receptor complex. When human fibrosarcoma cell lines deficient in Jak1, Jak2 or tyrosine kinase 2 (Tyk2) were stimulated with IL-6–soluble IL-6R complexes it was found that only in Jak1-, but not in Jak 2- or Tyk2-deficient cells, SHP2 activation was greatly impaired. It is concluded that Jak1 is required for the tyrosine phosphorylation of SHP2. This phosphorylation depends on Tyr-759 in the cytoplasmatic domain of gp130, since a Tyr-759 → Phe exchange abrogates SHP2 activation and in turn leads to elevated and prolonged STAT3 and STAT1 activation as well as enhanced acute-phase protein gene induction. Therefore, SHP2 plays an important role in acute-phase gene regulation.
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“In response to IL-6 SHP2 is rapidly recruited to gp130 [8] and phosphorylated by JAKs [11], which hints to a function as early feedback inhibitor.”
From The tyrosine phosphatase SHP2 increases robustness and information transfer within IL-6-induced JAK/STAT signalling (2021) · cites this paper as [11]
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“The lack of influence of SHP2 on robustness of late IL-6-induced STAT3 activation (Fig. 4) might be explained by the fact that SHP2 itself is phosphorylated rapidly in response to IL-6 (Fig. 1b) which causes dissociation from gp130 [9–11].”
From The tyrosine phosphatase SHP2 increases robustness and information transfer within IL-6-induced JAK/STAT signalling (2021) · cites this paper as [11]
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“also reported that over-expression of an inactive SHP-2 mutant in HepG2 cells enhanced STAT activation after IL-6 stimulation [15].”
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Bartoe, J. L., & Nathanson, N. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0742021.x · Cited by 24
“Work by Symes et al. (1997b) indicates that SHP-2 can negatively regulate the gp130-dependent induction of a VIP-luciferase reporter gene, and SHP-2 also negatively regulates the IL-6-dependent expression of acute-phase plasma proteins in hepatic cells (Kim et al., 1998; Schaper et al., 1998).”
BackgroundResultRolvering, C., Zimmer, A. D., Kozar, I., Hermanns, H. M., Letellier, E., Vallar, L., Nazarov, P. V., Nicot, N., Ginolhac, A., Haan, S., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.12.006 · Cited by 22
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“For example, the (SH2)-containing tyrosine phosphatase SHP-2 interacts specifically with JAK-1 and gp130 tyrosine residues (20, 21).”
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IL-35 and RANKL Synergistically Induce Osteoclastogenesis in RAW264 Mouse Monocytic Cells
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“In particular, the IL-6 signaling pathway downstream of JAK, corresponding to the MEK/ERK pathway, appears to play a critical role in the induction of c-Fos [34,35], which leads to activation of the osteoclast master regulatory transcriptional factor NF-ATc1 [36].”
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FAIRLIE, W. D., SOUZA, D. D., NICOLA, N. A., & BACA, M. (2003) · Biochemical Journal · doi:10.1042/bj20030104 · Cited by 20
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Self-citationGuillén, C., de Gortázar, A. R., & Esbrit, P. (2004) · Calcified Tissue International · doi:10.1007/s00223-004-0113-1 · Cited by 18
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“The wild-type EpoR/gp130 chimera and corresponding mutant chimeras containing tyrosineto-phenylalanine substitutions in conserved residues of the gp130 cytoplasmic domain were kind gifts of Dr. Fred Schaper, RWTH Aachen, Germany [Schaper et al., 1998; Schmitz et al., 2000].”
BackgroundMethodInfluentialThe Vesicular Stomatitis Virus Matrix Protein Inhibits Glycoprotein 130-Dependent STAT Activation
Terstegen, L., Gatsios, P., Ludwig, S., Pleschka, S., Jahnen‐Dechent, W., Heinrich, P. C., & Graeve, L. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.9.5209 · Cited by 15
“cDNAs for STAT3 tagged with a hemagglutinin (HA) epitope, Eg, and EgY759F (EgYFYYYY) were generated as described (6, 26, 27).”
BackgroundMethodInfluentialSelf-citationLing, P., Smith, R. J., Mueller, C., Mao, Y., & Bistrian, B. R. (2002) · Critical Care Medicine · doi:10.1097/00003246-200201000-00029 · Cited by 8
“These actions can be contrasted with those of the STAT pathways, which are largely responsible for the synthesis of acute phase proteins, many of which modulate and down-regulate proinflammatory components of the systemic inflammatory response (28, 29).”
BackgroundDifferential inhibition of IL‐6‐type cytokine‐induced STAT activation by PMA
Terstegen, L., Maassen, B. G., Radtke, S., Behrmann, I., Schaper, F., Heinrich, P. C., Graeve, L., & Gatsios, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01826-3 · Cited by 9
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“45,48,49 The Ras/Raf/MAPK signaling, primarily governs cell differentiation, thereby activating multiple transcriptional activators.”
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“Kinase inhibitionActivation of the IL-6 receptor complex by ligand binding triggers Janus kinase (JAK) autophosphorylation and activation, phosphorylation of specific intracellular tyrosine residues of the gp130 signaling subunit, recruitment of latent STAT3 via Src homology 2 (SH2) domain interactions, and ultimately…”
BackgroundIntragenic regulation of SOCS3 isoforms
Klepsch, O., Namer, L. S., Köhler, N., Kaempfer, R. O. R., Dittrich, A., & Schaper, F. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0379-6 · Cited by 11
Self-citationInterleukin-11, an IL-6-like cytokine
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“Under steady-state conditions, Ras/MAPK/Raf/Mek/Erk pathway activity is generally restrained but can be transiently activated by growth factors, such as FGF through FGFR as well as IGF through IGFR and LIF through gp130 [207].”
BackgroundProinflammatory Stem Cell Signaling in Cardiac Ischemia
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“SHP2 is recruited to the phosphotyrosine-759 residue of activated gp130 and is then tyrosine phosphorylated (72, 80, 123, 133).”
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“MAPK is an evolutionarily conserved group of silk/threonine protein kinases that, similar to STAT activation, are activated by activated LIF receptors (34).”
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“Although RHAMM is generally viewed as a pro-inflammatory mediator [70], it complexes with the kinase SHP2 [71] which is a negative regulator of inflammation [72,73].”
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Metadata
- Authors
- SCHAPER, F., GENDO, C., ECK, M., SCHMITZ, J., GRIMM, C., ANHUF, D., KERR, I. M., & HEINRICH, P. C.
- Affiliations
- RWTH Aachen University (DE)
- Department of Biochemistry, RWTH-Aachen, Pauwelsstraße 30, D52057 Aachen, Germany
- Imperial Cancer Research Fund, 44 Lincoln's Inns Field, London WC2A 3PX, U.K.
- Corresponding author
- SCHAPER, Fred
- GENDO, Cornelia
- SCHMITZ, Jochen
- GRIMM, Carsten
- ANHUF, Dirk
- ORCID
- SCHAPER, Fred
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1998-11-01
- Volume
- 335
- Issue
- 3
- Pages
- 557-565
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1219816
- OpenAlex
- W1939561089
- Cited by
- 178
- References
- 43
- Citations by year
- 2026: 1 · 2024: 5 · 2023: 1 · 2022: 2 · 2021: 5 · 2020: 7 · 2019: 7 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 4 · 2014: 8 · 2013: 5 · 2012: 6
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutscher Akademischer Austauschdienst
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › 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 › Protein Kinase Regulation and GTPase Signaling
- Keywords
- SHP2, protein tyrosine phosphatase, gp130, IL-6 signaling, JAK1, JAK2, TYK2, STAT3, STAT1, acute phase proteins, tyrosine phosphorylation, Grb2, RAS/RAF/MEK pathway, hepatic gene expression, fibrosarcoma cells
- MeSH terms
- DNA-Binding Proteins, Enzyme Activation, Carcinoma, Hepatocellular, Humans, Liver Neoplasms, Membrane Glycoproteins, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Tumor Cells, Cultured, Signal Transduction, Trans-Activators, Antigens, CD, Interleukin-6, Mutagenesis, Site-Directed, Protein Tyrosine Phosphatases, src Homology Domains, Receptors, Interleukin-6, Intracellular Signaling Peptides and Proteins, STAT3 Transcription Factor, Cytokine Receptor gp130, Janus Kinase 1, Janus Kinase 2, TYK2 Kinase, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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