Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-11-15
pubmed:databankReference
pubmed:abstractText
TRAF6 is a signal transducer in the NF-kappaB pathway that activates IkappaB kinase (IKK) in response to proinflammatory cytokines. We have purified a heterodimeric protein complex that links TRAF6 to IKK activation. Peptide mass fingerprinting analysis reveals that this complex is composed of the ubiquitin conjugating enzyme Ubc13 and the Ubc-like protein Uev1A. We find that TRAF6, a RING domain protein, functions together with Ubc13/Uev1A to catalyze the synthesis of unique polyubiquitin chains linked through lysine-63 (K63) of ubiquitin. Blockade of this polyubiquitin chain synthesis, but not inhibition of the proteasome, prevents the activation of IKK by TRAF6. These results unveil a new regulatory function for ubiquitin, in which IKK is activated through the assembly of K63-linked polyubiquitin chains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers, http://linkedlifedata.com/resource/pubmed/chemical/CHUK protein, human, http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase, http://linkedlifedata.com/resource/pubmed/chemical/IKBKB protein, human, http://linkedlifedata.com/resource/pubmed/chemical/IKBKE protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/Polyubiquitin, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 6, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/UBE2V1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-61
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11057907-Amino Acid Sequence, pubmed-meshheading:11057907-Biopolymers, pubmed-meshheading:11057907-Cell-Free System, pubmed-meshheading:11057907-Cloning, Molecular, pubmed-meshheading:11057907-Dimerization, pubmed-meshheading:11057907-Enzyme Activation, pubmed-meshheading:11057907-HeLa Cells, pubmed-meshheading:11057907-Humans, pubmed-meshheading:11057907-I-kappa B Kinase, pubmed-meshheading:11057907-Ligases, pubmed-meshheading:11057907-Molecular Sequence Data, pubmed-meshheading:11057907-Peptide Mapping, pubmed-meshheading:11057907-Polyubiquitin, pubmed-meshheading:11057907-Protein-Serine-Threonine Kinases, pubmed-meshheading:11057907-Proteins, pubmed-meshheading:11057907-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:11057907-TNF Receptor-Associated Factor 6, pubmed-meshheading:11057907-Transcription Factors, pubmed-meshheading:11057907-Ubiquitin-Conjugating Enzymes, pubmed-meshheading:11057907-Ubiquitin-Protein Ligases, pubmed-meshheading:11057907-Ubiquitins
pubmed:year
2000
pubmed:articleTitle
Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain.
pubmed:affiliation
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas 75390, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't