rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2000-2-29
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pubmed:abstractText |
We found previously that overexpression of an F-box protein betaTrCP1 and the structurally related betaTrCP2 augments ubiquitination of phosphorylated IkappaBalpha (pIkappaBalpha) induced by tumor necrosis factor-alpha (TNF-alpha), but the relationship of the two homologous betaTrCP proteins remains unknown. Herein we reveal that deletion mutants of betaTrCP1 and betaTrCP2 lacking the F-box domain suppressed ubiquitination and destruction of pIkappaBalpha as well as transcriptional activation of NF-kappaB. The ectopically expressed betaTrCP1 and betaTrCP2 formed both homodimer and heterodimer complexes without displaying the trimer complex. Dimerization of betaTrCP1 and/or betaTrCP2 takes place at their conserved NH(2)-terminal regions, termed a "D-domain" (for dimerization domain), located upstream of the F-box domain. The D-domain was necessary and sufficient for the dimer formation. Intriguingly, the betaTrCP homodimer, but not the heterodimer, was selectively recruited to pIkappaBalpha induced by TNF-alpha. These results indicate that not only betaTrCP1 but also betaTrCP2 participates in the ubiquitination-dependent destruction of IkappaBalpha by forming SCF(betaTrCP1-betaTrCP1) and SCF(betaTrCP2-betaTrCP2) ubiquitin-ligase complexes.
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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/BTRC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FBXW11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappaB inhibitor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Transducin Repeat-Containing...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2877-84
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10644755-Base Sequence,
pubmed-meshheading:10644755-Cell Line,
pubmed-meshheading:10644755-DNA Primers,
pubmed-meshheading:10644755-DNA-Binding Proteins,
pubmed-meshheading:10644755-Dimerization,
pubmed-meshheading:10644755-GTP-Binding Proteins,
pubmed-meshheading:10644755-Humans,
pubmed-meshheading:10644755-Hydrolysis,
pubmed-meshheading:10644755-I-kappa B Proteins,
pubmed-meshheading:10644755-Mutagenesis,
pubmed-meshheading:10644755-Protein Binding,
pubmed-meshheading:10644755-Sequence Deletion,
pubmed-meshheading:10644755-Signal Transduction,
pubmed-meshheading:10644755-Ubiquitin-Protein Ligases,
pubmed-meshheading:10644755-Ubiquitins,
pubmed-meshheading:10644755-beta-Transducin Repeat-Containing Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination.
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pubmed:affiliation |
Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Company Ltd., 21 Miyukigaoka, Tsukuba-shi, Ibaraki, 305-8585, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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