pubmed-article:19651900 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19651900 | lifeskim:mentions | umls-concept:C0011065 | lld:lifeskim |
pubmed-article:19651900 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
pubmed-article:19651900 | lifeskim:mentions | umls-concept:C1414315 | lld:lifeskim |
pubmed-article:19651900 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
pubmed-article:19651900 | lifeskim:mentions | umls-concept:C1538116 | lld:lifeskim |
pubmed-article:19651900 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:19651900 | pubmed:dateCreated | 2009-9-11 | lld:pubmed |
pubmed-article:19651900 | pubmed:abstractText | E3 ubiquitin ligases, which target specific molecules for proteolytic destruction, have emerged as key regulators of immune functions. Several E3 ubiquitin ligases, including c-Cbl, Cbl-b, GRAIL, Itch, and Nedd4, have been shown to negatively regulate T-cell activation. Here, we report that the HECT-type E3 ligase AIP2 positively regulates T-cell activation. Ectopic expression of AIP2 in mouse primary T cells enhances their proliferation and interleukin-2 production by suppressing the apoptosis of T cells. AIP2 interacts with and promotes ubiquitin-mediated degradation of EGR2, a zinc finger transcription factor that has been found to regulate Fas ligand (FasL) expression during activation-induced T-cell death. Suppression of AIP2 expression by small RNA interference upregulates EGR2, inhibits EGR2 ubiquitination and FasL expression, and enhances the apoptosis of T cells. Therefore, AIP2 regulates activation-induced T-cell death by suppressing EGR2-mediated FasL expression via the ubiquitin pathway. | lld:pubmed |
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pubmed-article:19651900 | pubmed:language | eng | lld:pubmed |
pubmed-article:19651900 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19651900 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:19651900 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19651900 | pubmed:month | Oct | lld:pubmed |
pubmed-article:19651900 | pubmed:issn | 1098-5549 | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:PeaEE | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:ChenAnA | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:YeShui QSQ | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:ZhangDonnaD | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:ZhangJingping... | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:GaoBeixueB | lld:pubmed |
pubmed-article:19651900 | pubmed:author | pubmed-author:McEwenTamaraT | lld:pubmed |
pubmed-article:19651900 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19651900 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:19651900 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19651900 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19651900 | pubmed:pagination | 5348-56 | lld:pubmed |
pubmed-article:19651900 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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pubmed-article:19651900 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19651900 | pubmed:articleTitle | The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell death by catalyzing EGR2 ubiquitination. | lld:pubmed |
pubmed-article:19651900 | pubmed:affiliation | Departments of Otolaryngology-Head and Neck Surgery and Molecular Microbiology and Immunology, University of Missouri-Columbia School of Medicine, One Hospital Dr., Columbia, MO 65212, USA. | lld:pubmed |