17095088

Source:http://linkedlifedata.com/resource/pubmed/id/17095088

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0086418, umls-concept:C0127400, umls-concept:C0330390, umls-concept:C1335874, umls-concept:C1415900, umls-concept:C1711351
pubmed:issue	8
pubmed:dateCreated	2006-12-4
pubmed:abstractText	CD4(+) T cells regulate adaptive responses to pathogens by secreting unique subsets of cytokines that mediate inflammatory processes. The innate cytokines IL-12 and IFN-alpha/beta regulate type I responses and promote acute IFN-gamma secretion through the activation of the STAT4 transcription factor. Although IL-12-induced STAT4 activation is a conserved pathway across species, IFN-alpha/beta-dependent STAT4 phosphorylation does not occur as efficiently in mice as it does in human T cells. In order to understand this species-specific pathway for IFN-alpha/beta-dependent STAT4 activation, we have examined the molecular basis of STAT4 recruitment by the human IFNAR. In this report, we demonstrate that the N-domain of STAT4 interacts with the cytoplasmic domain of the human, but not the murine IFNAR2 subunit. This interaction mapped to a membrane-proximal segment of the hIFNAR2 spanning amino acids 299-333. Deletion of this region within the hIFNAR2 completely abolishes IFN-alpha/beta-dependent STAT4 tyrosine phosphorylation when expressed in human IFNAR2-deficient fibroblasts. Thus, the human IFNAR2 cytoplasmic domain serves to link STAT4 to the IFNAR as a pre-assembled complex that facilitates cytokine-driven STAT4 activation.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/R01 AI056222-01A2, http://linkedlifedata.com/resource/pubmed/grant/R01 AI056222-02, http://linkedlifedata.com/resource/pubmed/grant/R01 AI056222-03
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7905289
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/IFNAR2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ifnar2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Interferon-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Interferon alpha-beta, http://linkedlifedata.com/resource/pubmed/chemical/STAT4 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/STAT4 protein, human
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	0161-5890
pubmed:author	pubmed-author:ChanSheuwenS, pubmed-author:FarrarJ DavidJD, pubmed-author:MatthewsLoderick ALA, pubmed-author:PerskyMeredith EME, pubmed-author:TylerDouglas RDR
pubmed:issnType	Print
pubmed:volume	44
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1864-72
pubmed:dateRevised	2011-9-26
pubmed:meshHeading	pubmed-meshheading:17095088-Animals, pubmed-meshheading:17095088-Cell Line, pubmed-meshheading:17095088-Fibroblasts, pubmed-meshheading:17095088-Humans, pubmed-meshheading:17095088-Interferon-alpha, pubmed-meshheading:17095088-Interferon-beta, pubmed-meshheading:17095088-Interleukin-12, pubmed-meshheading:17095088-Mice, pubmed-meshheading:17095088-Multiprotein Complexes, pubmed-meshheading:17095088-Phosphorylation, pubmed-meshheading:17095088-Protein Binding, pubmed-meshheading:17095088-Protein Processing, Post-Translational, pubmed-meshheading:17095088-Protein Structure, Tertiary, pubmed-meshheading:17095088-Receptor, Interferon alpha-beta, pubmed-meshheading:17095088-STAT4 Transcription Factor, pubmed-meshheading:17095088-Signal Transduction, pubmed-meshheading:17095088-Species Specificity
pubmed:year	2007
pubmed:articleTitle	Pre-assembly of STAT4 with the human IFN-alpha/beta receptor-2 subunit is mediated by the STAT4 N-domain.
pubmed:affiliation	Center for Immunology, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't