Linked Life Data

18180283

Source:http://linkedlifedata.com/resource/pubmed/id/18180283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2008-2-15
pubmed:abstractText
Interleukin 1 (IL-1) has been reported to stimulate the polyubiquitination and disappearance of IL-1 receptor-associated kinase 1 (IRAK1) within minutes. It has been thought that the polyubiquitin chains attached to IRAK1 are linked via Lys48 of ubiquitin, leading to its destruction by the proteasome and explaining the rapid IL-1-induced disappearance of IRAK1. In this paper, we demonstrate that IL-1 stimulates the formation of K63-pUb-IRAK1 and not K48-pUb-IRAK1 and that the IL-1-induced disappearance of IRAK1 is not blocked by inhibition of the proteasome. We also show that IL-1 triggers the interaction of K63-pUb-IRAK1 with NEMO, a regulatory subunit of the IkappaBalpha kinase (IKK) complex, but not with the NEMO[D311N] mutant that cannot bind K63-pUb chains. Moreover, unlike wild-type NEMO, the NEMO[D311N] mutant was unable to restore IL-1-stimulated NF-kappaB-dependent gene transcription to NEMO-deficient cells. Our data suggest a model in which the recruitment of the NEMO-IKK complex to K63-pUb-IRAK1 and the recruitment of the TAK1 complex to TRAF6 facilitate the TAK1-catalyzed activation of IKK by the TRAF6-IRAK1 complex.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-10215628, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-10373513, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-10395695, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11163183, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11242109, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11250893, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11259596, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11287640, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11460167, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11583588, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11788735, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-11937546, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-12496252, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-12667451, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-12860405, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-14592977, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-15169888, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-15199157, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-15327770, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-15485931, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-15833743, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16056267, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16186825, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16260493, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16371247, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16547522, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16603398, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-16884718, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-17197697, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-17635639, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-17675297, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-17997719, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-18021073, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-8524112, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-9261174, http://linkedlifedata.com/resource/pubmed/commentcorrection/18180283-9625767
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1098-5549
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1783-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18180283-Animals, pubmed-meshheading:18180283-Cell Line, pubmed-meshheading:18180283-Cells, Cultured, pubmed-meshheading:18180283-Embryo, Mammalian, pubmed-meshheading:18180283-Enzyme Activation, pubmed-meshheading:18180283-Fibroblasts, pubmed-meshheading:18180283-Genes, Reporter, pubmed-meshheading:18180283-Humans, pubmed-meshheading:18180283-I-kappa B Kinase, pubmed-meshheading:18180283-Interleukin-1, pubmed-meshheading:18180283-Interleukin-1 Receptor-Associated Kinases, pubmed-meshheading:18180283-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:18180283-Kidney, pubmed-meshheading:18180283-Luciferases, Firefly, pubmed-meshheading:18180283-Luciferases, Renilla, pubmed-meshheading:18180283-Lysine, pubmed-meshheading:18180283-Mice, pubmed-meshheading:18180283-Models, Biological, pubmed-meshheading:18180283-Mutation, pubmed-meshheading:18180283-Protein Binding, pubmed-meshheading:18180283-TNF Receptor-Associated Factor 6, pubmed-meshheading:18180283-Transfection, pubmed-meshheading:18180283-Ubiquitination
pubmed:year
2008
pubmed:articleTitle
Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase.
pubmed:affiliation
MRC Protein Phosphorylation Unit, College of Life Sciences, The Sir James Black Centre, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, United Kingdom.
pubmed:publicationType
Journal Article
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