Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
2003-6-30
pubmed:abstractText
The Toll/interleukin-1 receptor (TIR) family members play important roles in host defense. These receptors signal through TIR domain-containing adapter proteins. In this report, we identified a novel TIR domain-containing adapter protein designated as TIRP. Co-immunoprecipitation experiments suggest that TIRP is associated with IL-1 receptors. TIRP also interacts with kinase-inactive mutants of IRAK and IRAK-4, IRAK-2, IRAK-M, and TRAF6. Overexpression of TIRP activates NF-kappaB and potentiates IL-1 receptor-mediated NF-kappaB activation. A dominant negative mutant of TIRP inhibits IL-1- but not tumor necrosis factor-triggered NF-kappaB activation. Moreover, TIRP-mediated NF-kappaB activation is inhibited by dominant negative mutants of IRAK, IRAK-2, TRAF6, and IKKbeta. Our findings suggest that TIRP is involved in IL-1-triggered NF-kappaB activation and functions upstream of IRAK, IRAK-2, TRAF6, and IKKbeta
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular..., http://linkedlifedata.com/resource/pubmed/chemical/IRAK3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1 Receptor-Associated..., http://linkedlifedata.com/resource/pubmed/chemical/Irak3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1, http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24526-32
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12721283-Adaptor Proteins, Signal Transducing, pubmed-meshheading:12721283-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:12721283-Amino Acid Sequence, pubmed-meshheading:12721283-Humans, pubmed-meshheading:12721283-Interleukin-1, pubmed-meshheading:12721283-Interleukin-1 Receptor-Associated Kinases, pubmed-meshheading:12721283-Membrane Glycoproteins, pubmed-meshheading:12721283-Molecular Sequence Data, pubmed-meshheading:12721283-Mutation, pubmed-meshheading:12721283-Protein Kinases, pubmed-meshheading:12721283-Protein Structure, Tertiary, pubmed-meshheading:12721283-Receptors, Cell Surface, pubmed-meshheading:12721283-Receptors, Interleukin, pubmed-meshheading:12721283-Receptors, Interleukin-1, pubmed-meshheading:12721283-Sequence Alignment, pubmed-meshheading:12721283-Signal Transduction, pubmed-meshheading:12721283-Toll-Like Receptors
pubmed:year
2003
pubmed:articleTitle
TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing adapter protein involved in TIR signaling.
pubmed:affiliation
Department of Immunology, National Jewish Medical and Research Center, University of Colorado Health Sciences Center, Denver 80206, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't