Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-1-28
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Oxazoles, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STAT6 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/STAT6 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/calyculin A
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2787-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12426308-Base Sequence, pubmed-meshheading:12426308-CD4-Positive T-Lymphocytes, pubmed-meshheading:12426308-Cell Line, pubmed-meshheading:12426308-Enzyme Inhibitors, pubmed-meshheading:12426308-Humans, pubmed-meshheading:12426308-Interleukin-4, pubmed-meshheading:12426308-Jurkat Cells, pubmed-meshheading:12426308-Molecular Sequence Data, pubmed-meshheading:12426308-Oligodeoxyribonucleotides, pubmed-meshheading:12426308-Oxazoles, pubmed-meshheading:12426308-Phosphoprotein Phosphatases, pubmed-meshheading:12426308-Phosphorylation, pubmed-meshheading:12426308-Promoter Regions, Genetic, pubmed-meshheading:12426308-Protein Phosphatase 2, pubmed-meshheading:12426308-Recombinant Proteins, pubmed-meshheading:12426308-STAT6 Transcription Factor, pubmed-meshheading:12426308-Signal Transduction, pubmed-meshheading:12426308-Staurosporine, pubmed-meshheading:12426308-Trans-Activators, pubmed-meshheading:12426308-Transfection
pubmed:year
2003
pubmed:articleTitle
Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling.
pubmed:affiliation
Institute of Medical Microbiology and Immunology, University of Copenhagen, DK2200 Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't