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3. Sustained post-developmental T-bet expression is critical for the maintenance of type one innate lymphoid cells in vivo

Author

Schroeder, J-H, primary, Roberts, LB, additional, Meissl, K, additional, Lo, JW, additional, Hromadová, D, additional, Hayes, K, additional, Zabinski, T, additional, Read, E, additional, Heliodoro, C Moreira, additional, Reis, R, additional, Howard, JK, additional, Grencis, RK, additional, Neves, J F, additional, Strobl, B, additional, and Lord, GM, additional

Published
2021
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17. Benefit from participation in clinical trials

Author

Genss, EM, Janni, W, Kiechle, M, Sommer, H, Rack, B, Gauger, K, Heinrigs, M, Steinfeld, D, Augustin, D, Simon, W, Harbeck, N, Strobl, B, Dian, D, and Friese, K

Subjects
ddc: 610
Published
2006

18. The STAT3 isoforms alpha and beta have unique and specific functions

Author

Maritano, Diego, Sugrue, Ml, Tininini, S, Dewilde, Sarah, Strobl, B, Fu, X, MURRAY TAIT, V, Chiarle, Roberto, and Poli, Valeria

Subjects
Inflammation, STAT3 Transcription Factor, Stat3, Interleukin-6, Immunoblotting, Stat3 isoforms, Kidney, knock-in, isoform ablation, IL-6 signalling, gene targeting, inflammation, DNA-Binding Proteins, Mice, Fertility, Liver, Mutation, Trans-Activators, Animals, Protein Isoforms, Genes, Lethal, Lung
Abstract

Signal transducer and activator of transcription 3 (STAT3) is the main mediator of interleukin 6 (IL-6)-type cytokine signaling. It exists in two isoforms: the full-length STAT3 alpha and the truncated STAT3 beta, generally thought to act as a dominant negative factor. To assess their relative functions, we ablated the expression of either isoform by gene targeting. We show here that in vivo STAT3 beta is not a dominant negative factor. Its expression can rescue the embryonic lethality of a STAT3-null mutation and it can by itself induce the expression of specific STAT3 target genes. Nevertheless, STAT3 alpha has nonredundant roles such as modulation of cellular responses to IL-6 and mediation of IL-10 function in macrophages.

Published
2003

23. A completely foreign receptor can mediate an interferon-gamma-like response

Author

Strobl, B., Arulampalam, V., Isharc, H., Newman, S. J., Schlaak, J. F., Watling, D., Costa-Pereira, A. P., Schaper, F., Behrmann, Iris, Sheehan, K. C., Schreiber, R. D., Horn, F., Heinrich, P. C., Kerr, I. M., Strobl, B., Arulampalam, V., Isharc, H., Newman, S. J., Schlaak, J. F., Watling, D., Costa-Pereira, A. P., Schaper, F., Behrmann, Iris, Sheehan, K. C., Schreiber, R. D., Horn, F., Heinrich, P. C., and Kerr, I. M.

Abstract

A tripartite receptor comprising the external region of the erythropoietin (Epo) receptor, the transmembrane and JAK-binding domains of the gp130 subunit of the interleukin-6 (IL-6) receptor, and a seven amino acid STAT1 recruitment motif (Y440) from the interferon (IFN)-gamma receptor, efficiently mediates an IFN-gamma-like response. An analogous completely foreign chimeric receptor in which the Y440 motif is replaced with the Y905 motif from gp130 also mediates an IFN-gamma-like response, but less efficiently. The IFNGR1 signal-transducing subunit of the IFN-gamma receptor is tyrosine phosphorylated through the chimeric receptors and the endogenous IL-6 and OSM receptors. Cross phosphorylation of IFNGR1 is not, however, required for the IFN-gamma-like response through the chimeric receptors, nor does it mediate an IFN-gamma-like response to IL-6 or OSM. The data argue strongly for modular JAK/STAT signalling and against any rigid structural organization for the "pathways" involved. They emphasize the likely high degree of overlap between the signals generated from disparate JAK-receptor complexes and show that relatively minor changes in such complexes can profoundly affect the response.

Published
2001

24. A region encompassing the FERM domain of Jak1 is necessary for binding to the cytokine receptor gp130

Author

Hilkens, C. M., Isharc, H., Lillemeier, B. F., Strobl, B., Bates, P. A., Behrmann, Iris, Kerr, I. M., Hilkens, C. M., Isharc, H., Lillemeier, B. F., Strobl, B., Bates, P. A., Behrmann, Iris, and Kerr, I. M.

Abstract

The terminal portion of the Janus kinases (Jaks) contains a divergent FERM (Four-point-one, Ezrin, Radixin, Moesin) homology domain comprising 19 conserved hydrophobic regions. To determine the role of this domain in governing recruitment of Jak1, but not Jak3, to the gp130 subunit of the interleukin-6 family of cytokine receptors, the interaction of three Jak1/Jak3 chimeras with gp130 was investigated. Chimeras 1, 2 and 3 (Jak1 FERM regions 1-19, 1-18 and 1-8/Jak3, respectively) were all enzymically active. Chimeras 1 and 2 interacted with the cytoplasmic domain of gp130, although less efficiently than Jak1. Only chimera 2, however, restored gp130 signalling in Jak1-negative cells. The data are consistent with recruitment of Jak1 to gp130 through the Jak1 FERM domain, but also emphasise the likely requirement for precise Jak/receptor orientation to sustain function.

Published
2001
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