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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2000-11-3
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pubmed:abstractText |
The cytoplasmic domain of the human type I IFN receptor chain 2 (IFNAR2c or IFN-alphaRbetaL) was used as bait in a yeast two-hybrid system to identify novel proteins interacting with this region of the receptor. We report here a specific interaction between the cytoplasmic domain of IFN-alphaRbetaL and a previously identified protein, RACK-1 (receptor for activated C kinase). Using GST fusion proteins encoding different regions of the cytoplasmic domain of IFN-alphaRbetaL, the minimum site for RACK-1 binding was mapped to aa 300-346. RACK-1 binding to IFN-alphaRbetaL did not require the first 91 aa of RACK-1, which includes two WD domains, WD1 and WD2. The interaction between RACK-1 and IFN-alphaRbetaL, but not the human IFN receptor chain 1 (IFNAR1 or IFN-alphaRalpha), was also detected in human Daudi cells by coimmunoprecipitation. RACK-1 was shown to be constitutively associated with IFN-alphaRbetaL, and this association was not effected by stimulation of Daudi cells with type I IFNs (IFN-beta1b). RACK-1 itself did not become tyrosine phosphorylated upon stimulation of Daudi cells with IFN-beta1b. However, stimulation of cells with either IFN-beta1b or PMA did result in an increase in detectable immunofluorescence and intracellular redistribution of RACK-1.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/IFNAR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Interferon alpha-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/receptors for activated C kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
165
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5127-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11046044-Amino Acid Motifs,
pubmed-meshheading:11046044-Aspartic Acid,
pubmed-meshheading:11046044-Cell Line,
pubmed-meshheading:11046044-Enzyme Activation,
pubmed-meshheading:11046044-Humans,
pubmed-meshheading:11046044-Interferon Type I,
pubmed-meshheading:11046044-Intracellular Fluid,
pubmed-meshheading:11046044-Membrane Proteins,
pubmed-meshheading:11046044-Peptide Mapping,
pubmed-meshheading:11046044-Precipitin Tests,
pubmed-meshheading:11046044-Protein Binding,
pubmed-meshheading:11046044-Protein Kinase C,
pubmed-meshheading:11046044-Receptor, Interferon alpha-beta,
pubmed-meshheading:11046044-Receptors, Cell Surface,
pubmed-meshheading:11046044-Receptors, Interferon,
pubmed-meshheading:11046044-Repetitive Sequences, Amino Acid,
pubmed-meshheading:11046044-Saccharomyces cerevisiae,
pubmed-meshheading:11046044-Tetradecanoylphorbol Acetate,
pubmed-meshheading:11046044-Tryptophan,
pubmed-meshheading:11046044-Tumor Cells, Cultured,
pubmed-meshheading:11046044-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor.
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pubmed:affiliation |
Department of Immunology, Berlex Biosciences, Richmond CA 94804, USA. ed_croze@berlex.com
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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