Source:http://linkedlifedata.com/resource/pubmed/id/19706600
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
43
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pubmed:dateCreated |
2009-10-19
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pubmed:abstractText |
Ubiquitination-mediated degradation of the RelA subunit of nuclear factor-kappaB (NF-kappaB) is critical for the termination of NF-kappaB activation. However, the precise mechanism for the ubiquitination of RelA is still not fully understood. Here we report that tumor necrosis factor-alpha (TNFalpha) induces RelA polyubiquitination at the lysine 195 residue, and this ubiquitination event is critical for the degradation of RelA and termination of TNFalpha-mediated NF-kappaB activation. Overexpression of a RelA mutant with an arginine substitution for the lysine 195 residue dramatically inhibits RelA polyubiquitination and induces a stronger NF-kappaB activation compared with the wild type. Reconstitution of RelA-deficient mouse embryo fibroblast cells with wild-type RelA or RelA containing a K195R mutation revealed the importance of this site in TNFalpha-mediated RelA polyubiquitination, degradation, and attenuation of NF-kappaB activation. Our finding is the first report that substitution of a key RelA lysine residue with arginine inhibits TNFalpha-induced RelA ubiquitination and enhances TNFalpha-induced NF-kappaB activation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/RELA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Rela protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelA,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1083-351X
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pubmed:author |
pubmed-author:FanYihuiY,
pubmed-author:FuSongbinS,
pubmed-author:MaoRenfangR,
pubmed-author:ShiZhongchengZ,
pubmed-author:SongPingP,
pubmed-author:SunWenjingW,
pubmed-author:YangJianhuaJ,
pubmed-author:YangYuY,
pubmed-author:YvonEricE,
pubmed-author:ZhangDekaiD,
pubmed-author:ZhangHongH,
pubmed-author:ZhaoYanlingY
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29290-7
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pubmed:dateRevised |
2010-10-26
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pubmed:meshHeading |
pubmed-meshheading:19706600-Amino Acid Substitution,
pubmed-meshheading:19706600-Animals,
pubmed-meshheading:19706600-Cell Line,
pubmed-meshheading:19706600-Embryo, Mammalian,
pubmed-meshheading:19706600-Fibroblasts,
pubmed-meshheading:19706600-Humans,
pubmed-meshheading:19706600-Lysine,
pubmed-meshheading:19706600-Mice,
pubmed-meshheading:19706600-Mutation, Missense,
pubmed-meshheading:19706600-NF-kappa B,
pubmed-meshheading:19706600-Transcription Factor RelA,
pubmed-meshheading:19706600-Tumor Necrosis Factor-alpha,
pubmed-meshheading:19706600-Ubiquitination
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pubmed:year |
2009
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pubmed:articleTitle |
Tumor necrosis factor-alpha induces RelA degradation via ubiquitination at lysine 195 to prevent excessive nuclear factor-kappaB activation.
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pubmed:affiliation |
Department of Pediatrics, Texas Children's Cancer Center, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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