| pubmed-article:7479976 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7479976 | lifeskim:mentions | umls-concept:C0126732 | lld:lifeskim |
| pubmed-article:7479976 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:7479976 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:7479976 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:7479976 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:7479976 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:7479976 | pubmed:dateCreated | 1995-12-28 | lld:pubmed |
| pubmed-article:7479976 | pubmed:abstractText | The inhibitor protein I kappa B alpha controls the nuclear import of the transcription factor NF-kappa B. The inhibitory activity of I kappa B alpha is regulated from the cytoplasmic compartment by signal-induced proteolysis. Previous studies have shown that signal-dependent phosphorylation of serine residues 32 and 36 targets I kappa B alpha to the ubiquitin-proteasome pathway. Here we provide evidence that lysine residues 21 and 22 serve as the primary sites for signal-induced ubiquitination of I kappa B alpha. Conservative Lys-->Arg substitutions at both Lys-21 and Lys-22 produce dominant-negative mutants of I kappa B alpha in vivo. These constitutive inhibitors are appropriately phosphorylated but fail to release NF-kappa B in response to multiple inducers, including viral proteins, cytokines, and agents that mimic antigenic stimulation through the T-cell receptor. Moreover, these Lys-->Arg mutations prevent signal-dependent degradation of I kappa B alpha in vivo and ubiquitin conjugation in vitro. We conclude that site-specific ubiquitination of phosphorylated I kappa B alpha at Lys-21 and/or Lys-22 is an obligatory step in the activation of NF-kappa B. | lld:pubmed |
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| pubmed-article:7479976 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7479976 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7479976 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7479976 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7479976 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7479976 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7479976 | pubmed:author | pubmed-author:ChefRR | lld:pubmed |
| pubmed-article:7479976 | pubmed:author | pubmed-author:ManiatisTT | lld:pubmed |
| pubmed-article:7479976 | pubmed:author | pubmed-author:BrockmanJ AJA | lld:pubmed |
| pubmed-article:7479976 | pubmed:author | pubmed-author:BallardD WDW | lld:pubmed |
| pubmed-article:7479976 | pubmed:author | pubmed-author:SchererD CDC | lld:pubmed |
| pubmed-article:7479976 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7479976 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:7479976 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:7479976 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7479976 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7479976 | pubmed:pagination | 11259-63 | lld:pubmed |
| pubmed-article:7479976 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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