Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling

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Standard

Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling. / Woetmann, Anders; Brockdorff, Johannes; Lovato, Paola; Nielsen, Mette; Leick, Vagn; Rieneck, Klaus; Svejgaard, Arne; Geisler, Carsten; Ødum, Niels.

In: Journal of Biological Chemistry, Vol. 278, No. 5, 2002, p. 2787-91.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Woetmann, A, Brockdorff, J, Lovato, P, Nielsen, M, Leick, V, Rieneck, K, Svejgaard, A, Geisler, C & Ødum, N 2002, 'Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling', Journal of Biological Chemistry, vol. 278, no. 5, pp. 2787-91. https://doi.org/10.1074/jbc.M210196200

APA

Woetmann, A., Brockdorff, J., Lovato, P., Nielsen, M., Leick, V., Rieneck, K., Svejgaard, A., Geisler, C., & Ødum, N. (2002). Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling. Journal of Biological Chemistry, 278(5), 2787-91. https://doi.org/10.1074/jbc.M210196200

Vancouver

Woetmann A, Brockdorff J, Lovato P, Nielsen M, Leick V, Rieneck K et al. Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling. Journal of Biological Chemistry. 2002;278(5):2787-91. https://doi.org/10.1074/jbc.M210196200

Author

Woetmann, Anders ; Brockdorff, Johannes ; Lovato, Paola ; Nielsen, Mette ; Leick, Vagn ; Rieneck, Klaus ; Svejgaard, Arne ; Geisler, Carsten ; Ødum, Niels. / Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling. In: Journal of Biological Chemistry. 2002 ; Vol. 278, No. 5. pp. 2787-91.

Bibtex

@article{57ea9430b0a011ddb538000ea68e967b,
title = "Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling",
abstract = "Interleukin-4 (IL-4) plays a pivotal role in the induction and maintenance of allergy by promoting Th2 differentiation and B cell isotype switching to IgE. Studies on STAT6-deficient mice have demonstrated the essential role of STAT6 in mediating the biological functions of IL-4. IL-4 induces tyrosine phosphorylation of STAT6, which in turn leads to transcription of IL-4-specific genes. In addition, serine phosphorylation of STAT6 has recently been reported. Here we study the functional role of STAT6 serine phosphorylation and the kinases and phosphatases involved. We show that inhibition of protein phosphatase 2A (PP2A) induces serine phosphorylation of STAT6 and severely inhibits DNA binding of STAT6. In contrast, IL-4-induced tyrosine phosphorylation of Janus kinase-1 and STAT6 is not affected, suggesting that PP2A acts downstream of Janus kinases in IL-4 signaling. In conclusion, we provide the first evidence that PP2A plays a crucial role in the regulation of STAT6 function.",
author = "Anders Woetmann and Johannes Brockdorff and Paola Lovato and Mette Nielsen and Vagn Leick and Klaus Rieneck and Arne Svejgaard and Carsten Geisler and Niels {\O}dum",
note = "Keywords: Base Sequence; CD4-Positive T-Lymphocytes; Cell Line; Enzyme Inhibitors; Humans; Interleukin-4; Jurkat Cells; Molecular Sequence Data; Oligodeoxyribonucleotides; Oxazoles; Phosphoprotein Phosphatases; Phosphorylation; Promoter Regions (Genetics); Protein Phosphatase 2; Recombinant Proteins; STAT6 Transcription Factor; Signal Transduction; Staurosporine; Trans-Activators; Transfection",
year = "2002",
doi = "10.1074/jbc.M210196200",
language = "English",
volume = "278",
pages = "2787--91",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling

AU - Woetmann, Anders

AU - Brockdorff, Johannes

AU - Lovato, Paola

AU - Nielsen, Mette

AU - Leick, Vagn

AU - Rieneck, Klaus

AU - Svejgaard, Arne

AU - Geisler, Carsten

AU - Ødum, Niels

N1 - Keywords: Base Sequence; CD4-Positive T-Lymphocytes; Cell Line; Enzyme Inhibitors; Humans; Interleukin-4; Jurkat Cells; Molecular Sequence Data; Oligodeoxyribonucleotides; Oxazoles; Phosphoprotein Phosphatases; Phosphorylation; Promoter Regions (Genetics); Protein Phosphatase 2; Recombinant Proteins; STAT6 Transcription Factor; Signal Transduction; Staurosporine; Trans-Activators; Transfection

PY - 2002

Y1 - 2002

N2 - Interleukin-4 (IL-4) plays a pivotal role in the induction and maintenance of allergy by promoting Th2 differentiation and B cell isotype switching to IgE. Studies on STAT6-deficient mice have demonstrated the essential role of STAT6 in mediating the biological functions of IL-4. IL-4 induces tyrosine phosphorylation of STAT6, which in turn leads to transcription of IL-4-specific genes. In addition, serine phosphorylation of STAT6 has recently been reported. Here we study the functional role of STAT6 serine phosphorylation and the kinases and phosphatases involved. We show that inhibition of protein phosphatase 2A (PP2A) induces serine phosphorylation of STAT6 and severely inhibits DNA binding of STAT6. In contrast, IL-4-induced tyrosine phosphorylation of Janus kinase-1 and STAT6 is not affected, suggesting that PP2A acts downstream of Janus kinases in IL-4 signaling. In conclusion, we provide the first evidence that PP2A plays a crucial role in the regulation of STAT6 function.

AB - Interleukin-4 (IL-4) plays a pivotal role in the induction and maintenance of allergy by promoting Th2 differentiation and B cell isotype switching to IgE. Studies on STAT6-deficient mice have demonstrated the essential role of STAT6 in mediating the biological functions of IL-4. IL-4 induces tyrosine phosphorylation of STAT6, which in turn leads to transcription of IL-4-specific genes. In addition, serine phosphorylation of STAT6 has recently been reported. Here we study the functional role of STAT6 serine phosphorylation and the kinases and phosphatases involved. We show that inhibition of protein phosphatase 2A (PP2A) induces serine phosphorylation of STAT6 and severely inhibits DNA binding of STAT6. In contrast, IL-4-induced tyrosine phosphorylation of Janus kinase-1 and STAT6 is not affected, suggesting that PP2A acts downstream of Janus kinases in IL-4 signaling. In conclusion, we provide the first evidence that PP2A plays a crucial role in the regulation of STAT6 function.

U2 - 10.1074/jbc.M210196200

DO - 10.1074/jbc.M210196200

M3 - Journal article

C2 - 12426308

VL - 278

SP - 2787

EP - 2791

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 5

ER -

ID: 8544491