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• W1988559504 abstract "The human interleukin-3 receptor (hIL-3R) consists of a unique α subunit (hIL-3Rα) and a common β subunit (βc). Binding of IL-3 to IL-3R activates Janus kinases JAK1 and JAK2. Our previously study showed that JAK2 and JAK1 were constitutively associated with the hIL-3Rα and βc subunits, respectively. In this study, we further demonstrate that JAK2 binds to the intracellular domain of hIL-3Rα and JAK1 binds to the Box 1 and Box 2 motifs of βc using GST-hIL-3R fusion proteins in pull-down assays. JAK1 mutational analysis revealed that its JH7-3 domains bound directly to the Box 1 and Box 2 motifs of βc. We further examined the role of JAK1 JH7-3 domains in JAK1 and JAK2-mediated signaling using the CDJAKs fusion proteins, which consisted of a CD16 extracellular domain, a CD7 transmembrane domain, and either JAK1 (CDJAK1), JAK2 (CDJAK2), or JAK1-JH7-3 domains (CDJAK1-JH7-3) as intracellular domains. Anti-CD16 antibody crosslinking of wild type fusion proteins CDJAK1 with CDJAK2 could mimic IL-3 signaling, however, the crosslinking of fusion proteins CDJAK1-JH7-3 with CDJAK2 failed to activate downstream proteins. These results suggest that the JAK1-JH7-3 domains are required for βc interaction and abolish wild type JAK1 and JAK2-mediated signaling. J. Cell. Biochem. 99: 1078–1084, 2006. © 2006 Wiley-Liss, Inc." @default.
• W1988559504 created "2016-06-24" @default.
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• W1988559504 date "2006-01-01" @default.
• W1988559504 modified "2023-10-17" @default.
• W1988559504 title "JAK1 N-terminus binds to conserved box 1 and box 2 motifs of cytokine receptor common β subunit but signal activation requires JAK1 C-terminus" @default.
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• W1988559504 doi "https://doi.org/10.1002/jcb.20942" @default.
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