Jak-Stat signal transduction pathway through the eyes of cytokine class II receptor complexes

Kotenko, Sergei V.; Pestka, Sidney

doi:10.1038/sj.onc.1203524

Cited by 191 publications

(137 citation statements)

References 112 publications

(106 reference statements)

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“…It has also been shown that, despite their different biological activities, some of these cytokines share their receptors with each other and sometimes utilize the same ones. For example, the second receptor of IL-10, IL-10R2, is involved in the formation of signaling complexes of not only IL-10 but also IL-22 and INF-λs, whereas the first receptor of IL-22, IL-22R1, also participates in a complex formation induced by IL-20 and IL-24 (21)(22)(23)(24). Both IL-20 and IL-24 form complexes with the receptor pair IL-22R1/IL-20R2 (25).…”

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confidence: 99%

Characterization of the Recombinant Extracellular Domains of Human Interleukin-20 Receptors and Their Complexes with Interleukin-19 and Interleukin-20

et al. 2003

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The soluble extracellular domains of human interleukin-20 (IL-20) receptors I and II (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells and purified to homogeneity. Formation of the receptor/receptor and ligand/receptor complexes was studied by size exclusion chromatography. Both ligands and soluble receptors were found to be monomeric in solution; homo-or heterodimers are not formed even at elevated concentrations. Under native conditions, both IL-19 and IL-20 form stable ternary 1:1:1 complexes with the sIL-20R1 and sIL20R2 receptors, as well as high-affinity binary complexes with sIL-20R2. Unexpectedly, sIL-20R1 does not bind on its own to either IL-19 or IL-20. Thus, one of the possible consecutive mechanisms of formation of the signaling ternary complex may involve two steps: first, the ligand binds to receptor II, creating a high-affinity binding site for the receptor I, and only then does receptor I complete the complex.

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confidence: 99%

Characterization of the Recombinant Extracellular Domains of Human Interleukin-20 Receptors and Their Complexes with Interleukin-19 and Interleukin-20

et al. 2003

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“…CRF2-9 was originally described as an orphan receptor called ZCYTOR11 in patent databases and proposed to be renamed IL-22R by Xie et al (3). Both chains belong to the class II cytokine receptor family (7). This family consists of eight members, including two pairs of two receptor subunits for either type I (IFN-␣, IFN-␤, IFN-, and IFN-) and type II (IFN-␥) IFNs, the IL-10R, the IL-22R/CRF2-9, the IL-10R␤/CRF2-4, the IL-20R/ CRF2-8, and tissue factor (TF) (7,8).…”

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confidence: 99%

“…Both chains belong to the class II cytokine receptor family (7). This family consists of eight members, including two pairs of two receptor subunits for either type I (IFN-␣, IFN-␤, IFN-, and IFN-) and type II (IFN-␥) IFNs, the IL-10R, the IL-22R/CRF2-9, the IL-10R␤/CRF2-4, the IL-20R/ CRF2-8, and tissue factor (TF) (7,8). These receptors are almost exclusively related by their extracellular domain, which have tandem fibronectin type III (FNIII) domains.…”

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confidence: 99%

Cloning and Characterization of IL-22 Binding Protein, a Natural Antagonist of IL-10-Related T Cell-Derived Inducible Factor/IL-22

Dumoutier

Lejeune

Colau

et al. 2001

The Journal of Immunology

234

211

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The class II cytokine receptor family includes the receptors for IFN-αβ, IFN-γ, IL-10, and IL-10-related T cell-derived inducible factor/IL-22. By screening genomic DNA databases, we identified a gene encoding a protein of 231 aa, showing 33 and 34% amino acid identity with the extracellular domains of the IL-22 receptor and of the IL-20R/cytokine receptor family 2-8, respectively, but lacking the transmembrane and cytoplasmic domains. A lower but significant sequence identity was found with other members of this family such as the IL-10R (29%), cytokine receptor family 2-4/IL-10Rβ (30%), tissue factor (26%), and the four IFN receptor chains (23–25%). This gene is located on chromosome 6q24, at 35 kb from the IFNGR1 gene, and is expressed in various tissues with maximal expression in breast, lungs, and colon. The recombinant protein was found to bind IL-10-related T cell-derived inducible factor/IL-22, and to inhibit the activity of this cytokine on hepatocytes and intestinal epithelial cells. We propose to name this natural cytokine antagonist IL-22BP for IL-22 binding protein.

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“…The family of type II cytokine receptor molecules (29) comprises a series of initially orphan receptor chains in addition to the prototypic heterodimeric receptor for IL-10. The IL-10 receptor (IL-10R) consists of a long transmembrane chain (IL-10R1, Ref.…”

mentioning

confidence: 99%

The T-cell Lymphokine Interleukin-26 Targets Epithelial Cells through the Interleukin-20 Receptor 1 and Interleukin-10 Receptor 2 Chains

Hör

Pirzer

Dumoutier

et al. 2004

Journal of Biological Chemistry

127

116

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Jak-Stat signal transduction pathway through the eyes of cytokine class II receptor complexes

Cited by 191 publications

References 112 publications

Characterization of the Recombinant Extracellular Domains of Human Interleukin-20 Receptors and Their Complexes with Interleukin-19 and Interleukin-20

Characterization of the Recombinant Extracellular Domains of Human Interleukin-20 Receptors and Their Complexes with Interleukin-19 and Interleukin-20

Cloning and Characterization of IL-22 Binding Protein, a Natural Antagonist of IL-10-Related T Cell-Derived Inducible Factor/IL-22

The T-cell Lymphokine Interleukin-26 Targets Epithelial Cells through the Interleukin-20 Receptor 1 and Interleukin-10 Receptor 2 Chains

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