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| Home > Publications database > Tryptophan (W) at position 37 of murine IL-12/IL-23 p40 is mandatory for binding to IL-12Rβ1 and subsequent signal transduction > print |
| Home > Publications database > Tryptophan (W) at position 37 of murine IL-12/IL-23 p40 is mandatory for binding to IL-12Rβ1 and subsequent signal transduction > print |
| 001 | 904312 | ||
| 005 | 20220103172037.0 | ||
| 024 | 7 | _ | |a 10.1016/j.jbc.2021.101295 |2 doi |
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| 100 | 1 | _ | |a Georgy, Jacqueline |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Tryptophan (W) at position 37 of murine IL-12/IL-23 p40 is mandatory for binding to IL-12Rβ1 and subsequent signal transduction |
| 260 | _ | _ | |a Bethesda, Md. |c 2021 |b Soc. |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Interleukin (IL)-12 and IL-23 are composite cytokines consisting of p35/p40 and p19/p40, respectively, which signal via the common IL-12 receptor β1 (IL-12Rβ1) and the cytokine-specific receptors IL-12Rβ2 and IL-23R. Previous data showed that the p40 component interacts with IL-12Rβ1, whereas p19 and p35 subunits solely bind to IL-23R and IL-12Rβ2, resulting in tetrameric signaling complexes. In the absence of p19 and p35, p40 forms homodimers and may induce signaling via IL-12Rβ1 homodimers. The critical amino acids of p19 and p35 required for binding to IL-23R and IL-12Rβ2 are known, and two regions of p40 critical for binding to IL-12Rβ1 have recently been identified. In order to characterize the involvement of the N-terminal region of p40 in binding to IL-12Rβ1, we generated deletion variants of the p40-p19 fusion cytokine. We found that an N-terminal deletion variant missing amino acids M23 to P39 failed to induce IL-23-dependent signaling and did not bind to IL-12Rβ1, whereas binding to IL-23R was maintained. Amino acid replacements showed that p40W37K largely abolished IL-23-induced signal transduction and binding to IL-12Rβ1, but not binding to IL-23R. Combining p40W37K with D36K and T38K mutations eliminated the biological activity of IL-23. Finally, homodimeric p40D36K/W37K/T38K did not interact with IL-12Rβ1, indicating binding of homodimeric p40 to IL-12Rβ1 is comparable to the interaction of IL-23/IL-12 and IL-12Rβ1. In summary, we have defined D36, W37, and T38 as hotspot amino acids for the interaction of IL-12/IL-23 p40 with IL-12Rβ1. Structural insights into cytokine–cytokine receptor binding are important to develop novel therapeutic strategies. |
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| 700 | 1 | _ | |a Ouzin, Meryem |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Weitz, Hendrik T. |0 0000-0002-7185-0016 |b 4 |
| 700 | 1 | _ | |a Gremer, Lothar |0 P:(DE-Juel1)145165 |b 5 |
| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 6 |
| 700 | 1 | _ | |a Grötzinger, Joachim |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Thives-Kurenbach, Felix |0 P:(DE-HGF)0 |b 8 |
| 700 | 1 | _ | |a Scheller, Jürgen |0 0000-0001-9932-1055 |b 9 |
| 700 | 1 | _ | |a Floss, Doreen M. |0 0000-0002-6675-5313 |b 10 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.jbc.2021.101295 |g Vol. 297, no. 5, p. 101295 - |0 PERI:(DE-600)1474604-9 |n 5 |p 101295 - |t The journal of biological chemistry |v 297 |y 2021 |x 0021-9258 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/904312/files/1-s2.0-S0021925821011017-main.pdf |y OpenAccess |
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