Roles of JAK kinases in human GM-CSF receptor signal transduction

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Roles of JAK kinases in human GM-CSF receptor signal transduction Sumiko Watanabe, PhD, Tohru Itoh, MSc, Ken-ichi Arai, MD, PhD Journal of Allergy and Clinical Immunology Volume 98, Issue 6, Pages S183-S191 (December 1996) DOI: 10.1016/S0091-6749(96)70065-9 Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 1 Analysis of requirements of tyrosine residues of hGMR on various signals. A, Schematic drawing of various hGMRβ mutants. B, Activation of c-fos promoter through various C-terminal deletion mutants of hGMRβ. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 1 Analysis of requirements of tyrosine residues of hGMR on various signals. A, Schematic drawing of various hGMRβ mutants. B, Activation of c-fos promoter through various C-terminal deletion mutants of hGMRβ. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 2 Effects of tyrosine residue substitution in hGMRβ on Shc and SHP-2(PTP 1D) phosphorylation. A, c-fos-luciferase activity in the BA/F3 cells expressing hGMRα and various mutants of hGMRβ. BA/F3 cells expressing hGMRα and various mutants of hGMRβ were depleted of mIL-5 for 5 hours and restimulated with hGM-CSF for 5 minutes. Cells were lysed and total proteins (B) or proteins immunoprecipitated by either anti-Shc or anti-SHP-2(PTP 1D) antibodies (C) were analyzed using Western blotting. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 2 Effects of tyrosine residue substitution in hGMRβ on Shc and SHP-2(PTP 1D) phosphorylation. A, c-fos-luciferase activity in the BA/F3 cells expressing hGMRα and various mutants of hGMRβ. BA/F3 cells expressing hGMRα and various mutants of hGMRβ were depleted of mIL-5 for 5 hours and restimulated with hGM-CSF for 5 minutes. Cells were lysed and total proteins (B) or proteins immunoprecipitated by either anti-Shc or anti-SHP-2(PTP 1D) antibodies (C) were analyzed using Western blotting. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 2 Effects of tyrosine residue substitution in hGMRβ on Shc and SHP-2(PTP 1D) phosphorylation. A, c-fos-luciferase activity in the BA/F3 cells expressing hGMRα and various mutants of hGMRβ. BA/F3 cells expressing hGMRα and various mutants of hGMRβ were depleted of mIL-5 for 5 hours and restimulated with hGM-CSF for 5 minutes. Cells were lysed and total proteins (B) or proteins immunoprecipitated by either anti-Shc or anti-SHP-2(PTP 1D) antibodies (C) were analyzed using Western blotting. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 3 Requirements of box1, box2 region for various hGM-CSF activities. A, Effects of deletion of either box1 or box2 on c-fos (A) or c-myc (B) and egr-1 (C) promoter activations by hGM-CSF. BA/F3 cells expressing wild type hGMRα and hGMRβ mutants lacking either the box1 or box2 were transfected by c-fos-luciferase, c-myc -CAT, or egr-1-CAT plasmids. Activation of these promoters by hGM-CSF was analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 3 Requirements of box1, box2 region for various hGM-CSF activities. A, Effects of deletion of either box1 or box2 on c-fos (A) or c-myc (B) and egr-1 (C) promoter activations by hGM-CSF. BA/F3 cells expressing wild type hGMRα and hGMRβ mutants lacking either the box1 or box2 were transfected by c-fos-luciferase, c-myc -CAT, or egr-1-CAT plasmids. Activation of these promoters by hGM-CSF was analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 3 Requirements of box1, box2 region for various hGM-CSF activities. A, Effects of deletion of either box1 or box2 on c-fos (A) or c-myc (B) and egr-1 (C) promoter activations by hGM-CSF. BA/F3 cells expressing wild type hGMRα and hGMRβ mutants lacking either the box1 or box2 were transfected by c-fos-luciferase, c-myc -CAT, or egr-1-CAT plasmids. Activation of these promoters by hGM-CSF was analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 4 Phosphorylation of hGMRβ and cellular proteins through hGMRβ mutants. Total proteins (b) or immunoprecipitants of hGMRβ (a) were electrophoresed and tyrosine phosphorylation was analyzed using Western blotting using anti-phospho-tyrosine antibody or anti β-chain antibody. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 5 Effect of dominant negative JAK2 in various activities by hGMR. A, Phosphorylation of JAK2 and STAT5 in the presence or absence of ΔJAK2. Plasmids encoding hGMRα and β were transfected to BA/F3 cells with either vector control or ΔJAK2. JAK2 or STAT5 proteins were immunoprecipitated and analyzed with Western blotting using anti-phospho tyrosine antibody 4G10. B, Effects of ΔJAK2 for c-myc promoter activation and proliferation. ΔJAK2 was cotransfected with c-myc CAT plasmid in BA/FGMR cells and CAT activity induced by either mIL-3 Shaded Box or hGM-CSF Solid Square was analyzed using diffusion analysis. Plasmids encoding hGMRα and β subunits were transfected to BA/F3 cells with or without ΔJAK2 plasmids and proliferation activity was analyzed using MTT analysis. C, hGM-CSF induced c-fos and egr-1 promoter activation in the presence of dominant negative JAK2. c-fos-luciferase or egr-1-CAT plasmids were transfected to BA/FGMR cells with and without ΔJAK2, and luciferase or CAT activities induced by mIL-3 Shaded Box or hGM-CSF Solid Square were analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 5 Effect of dominant negative JAK2 in various activities by hGMR. A, Phosphorylation of JAK2 and STAT5 in the presence or absence of ΔJAK2. Plasmids encoding hGMRα and β were transfected to BA/F3 cells with either vector control or ΔJAK2. JAK2 or STAT5 proteins were immunoprecipitated and analyzed with Western blotting using anti-phospho tyrosine antibody 4G10. B, Effects of ΔJAK2 for c-myc promoter activation and proliferation. ΔJAK2 was cotransfected with c-myc CAT plasmid in BA/FGMR cells and CAT activity induced by either mIL-3 Shaded Box or hGM-CSF Solid Square was analyzed using diffusion analysis. Plasmids encoding hGMRα and β subunits were transfected to BA/F3 cells with or without ΔJAK2 plasmids and proliferation activity was analyzed using MTT analysis. C, hGM-CSF induced c-fos and egr-1 promoter activation in the presence of dominant negative JAK2. c-fos-luciferase or egr-1-CAT plasmids were transfected to BA/FGMR cells with and without ΔJAK2, and luciferase or CAT activities induced by mIL-3 Shaded Box or hGM-CSF Solid Square were analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 5 Effect of dominant negative JAK2 in various activities by hGMR. A, Phosphorylation of JAK2 and STAT5 in the presence or absence of ΔJAK2. Plasmids encoding hGMRα and β were transfected to BA/F3 cells with either vector control or ΔJAK2. JAK2 or STAT5 proteins were immunoprecipitated and analyzed with Western blotting using anti-phospho tyrosine antibody 4G10. B, Effects of ΔJAK2 for c-myc promoter activation and proliferation. ΔJAK2 was cotransfected with c-myc CAT plasmid in BA/FGMR cells and CAT activity induced by either mIL-3 Shaded Box or hGM-CSF Solid Square was analyzed using diffusion analysis. Plasmids encoding hGMRα and β subunits were transfected to BA/F3 cells with or without ΔJAK2 plasmids and proliferation activity was analyzed using MTT analysis. C, hGM-CSF induced c-fos and egr-1 promoter activation in the presence of dominant negative JAK2. c-fos-luciferase or egr-1-CAT plasmids were transfected to BA/FGMR cells with and without ΔJAK2, and luciferase or CAT activities induced by mIL-3 Shaded Box or hGM-CSF Solid Square were analyzed. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions

FIG. 6 Phosphorylation of various mutants and wild type of hGMRβ subunits in COS7 cells in the presence of JAK2. Plasmids encoding wild type or various mutants of hGMRβ were transfected to COS7 cells with JAK2 plasmid and phosphorylation of these receptors was analyzed using immunoprecipitation followed by immunoblotting. Journal of Allergy and Clinical Immunology 1996 98, S183-S191DOI: (10.1016/S0091-6749(96)70065-9) Copyright © 1996 Mosby, Inc. Terms and Conditions