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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 |
2005-4-21
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pubmed:abstractText |
TRAC-1 (T cell RING (really interesting new gene) protein identified in activation screen) is a novel E3 ubiquitin ligase identified from a retroviral vector-based T cell surface activation marker screen. The C-terminal truncated TRAC-1 specifically inhibited anti-TCR-mediated CD69 up-regulation in Jurkat cells, a human T leukemic cell line. In this study, we show that TRAC-1 is a RING finger ubiquitin E3 ligase with highest expression in lymphoid tissues. Point mutations that disrupt the Zn(2+)-chelating ability of its amino-terminal RING finger domain abolished TRAC-1's ligase activity and the dominant inhibitory effect of C-terminal truncated TRAC-1 on TCR stimulation. The results of in vitro biochemical studies indicate that TRAC-1 can stimulate the formation of both K48- and K63-linked polyubiquitin chains and therefore could potentially activate both degradative and regulatory ubiquitin-dependent pathways. Antisense oligonucleotides to TRAC-1 specifically reduced TRAC-1 mRNA levels in Jurkat and primary T cells and inhibited their activation in response to TCR cross-linking. Collectively, these results indicate that the E3 ubiquitin ligase TRAC-1 functions as a positive regulator of T cell activation.
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NCOR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Co-Repressor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Polyubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/UBC13 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/UBE2D3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/UBE2V1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1767
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pubmed:author |
pubmed-author:BennettMark KMK,
pubmed-author:ChuPeter CPC,
pubmed-author:Daniel-IssakaniSarkizS,
pubmed-author:DongJohn GJG,
pubmed-author:HuangBettyB,
pubmed-author:HuangJianingJ,
pubmed-author:HuangQiQ,
pubmed-author:LiConnie CCC,
pubmed-author:LiaoCharlene XCX,
pubmed-author:LuHenryH,
pubmed-author:MasudaEsteban SES,
pubmed-author:MolineauxSusan MSM,
pubmed-author:PardoJorgeJ,
pubmed-author:PayanDonald GDG,
pubmed-author:ZhaoHaoranH,
pubmed-author:ZhouXiulanX
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
174
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5288-97
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15843525-Amino Acid Motifs,
pubmed-meshheading:15843525-Amino Acid Sequence,
pubmed-meshheading:15843525-Base Sequence,
pubmed-meshheading:15843525-Catalysis,
pubmed-meshheading:15843525-Cell Cycle Proteins,
pubmed-meshheading:15843525-Cell Line,
pubmed-meshheading:15843525-Cell Line, Tumor,
pubmed-meshheading:15843525-DNA-Binding Proteins,
pubmed-meshheading:15843525-Humans,
pubmed-meshheading:15843525-Jurkat Cells,
pubmed-meshheading:15843525-Lymphocyte Activation,
pubmed-meshheading:15843525-Lymphoid Tissue,
pubmed-meshheading:15843525-Molecular Sequence Data,
pubmed-meshheading:15843525-Nuclear Proteins,
pubmed-meshheading:15843525-Nuclear Receptor Co-Repressor 2,
pubmed-meshheading:15843525-Peptide Fragments,
pubmed-meshheading:15843525-Polyubiquitin,
pubmed-meshheading:15843525-Receptors, Antigen, T-Cell,
pubmed-meshheading:15843525-Repressor Proteins,
pubmed-meshheading:15843525-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15843525-Signal Transduction,
pubmed-meshheading:15843525-T-Lymphocytes,
pubmed-meshheading:15843525-Transcription Factors,
pubmed-meshheading:15843525-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:15843525-Ubiquitin-Protein Ligases,
pubmed-meshheading:15843525-Up-Regulation
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pubmed:year |
2005
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pubmed:articleTitle |
A novel E3 ubiquitin ligase TRAC-1 positively regulates T cell activation.
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pubmed:affiliation |
Rigel Pharmaceuticals, Inc., South San Francisco, CA 94080, USA. hzhao@rigel.com
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pubmed:publicationType |
Journal Article
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