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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2001-5-22
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pubmed:abstractText |
The T cell death associated gene 51 (TDAG51) was shown to be required for T cell receptor (TCR)-dependent induction of Fas/Apo1/CD95 expression in a murine T cell hybridoma. Despite the absence of a nuclear localization sequence and a nucleic acid binding domain, it was suggested to be localized in the nucleus and to function as a transcription factor regulating Fas-expression. However, we demonstrate that the human (h)TDAG51 protein is localized in the cytoplasm and the nucleoli, suggesting a role in ribosome biogenesis and/or translation regulation. Indeed, it strongly inhibited translation of a luciferase mRNA in a reticulocyte translational extract. Furthermore, cotransfection of hTDAG51 and the luciferase gene into 293T cells resulted in a strong inhibition of luciferase mRNA translation. Our findings were further strengthened by isolating in a yeast two-hybrid screen three proteins which are involved in the regulation of translation. We speculate that hTDAG51 couples TCR signaling to inhibition of protein biosynthesis in activated T lymphocytes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/PHLDA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(A)-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prokaryotic Initiation Factor-3,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L14
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0898-6568
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
345-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11369516-Animals,
pubmed-meshheading:11369516-Apoptosis,
pubmed-meshheading:11369516-B-Lymphocytes,
pubmed-meshheading:11369516-Cell Line, Transformed,
pubmed-meshheading:11369516-Cell Nucleolus,
pubmed-meshheading:11369516-Gene Expression,
pubmed-meshheading:11369516-Humans,
pubmed-meshheading:11369516-Hybridomas,
pubmed-meshheading:11369516-Luciferases,
pubmed-meshheading:11369516-Mammals,
pubmed-meshheading:11369516-Peptide Initiation Factors,
pubmed-meshheading:11369516-Poly(A)-Binding Proteins,
pubmed-meshheading:11369516-Prokaryotic Initiation Factor-3,
pubmed-meshheading:11369516-Protein Biosynthesis,
pubmed-meshheading:11369516-RNA, Messenger,
pubmed-meshheading:11369516-RNA-Binding Proteins,
pubmed-meshheading:11369516-Receptors, Antigen, T-Cell,
pubmed-meshheading:11369516-Ribosomal Proteins,
pubmed-meshheading:11369516-Signal Transduction,
pubmed-meshheading:11369516-T-Lymphocytes,
pubmed-meshheading:11369516-Transcription Factors,
pubmed-meshheading:11369516-Two-Hybrid System Techniques,
pubmed-meshheading:11369516-Yeasts
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pubmed:year |
2001
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pubmed:articleTitle |
Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product.
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pubmed:affiliation |
Department of Immunology, Paul-Ehrlich-Institute, Paul-Ehrlich-Stasse 51-59, D-63225, Langen, Germany. hinth@pei.de
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pubmed:publicationType |
Journal Article,
In Vitro
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