Linked Life Data

10781837

Source:http://linkedlifedata.com/resource/pubmed/id/10781837

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-6-29
pubmed:abstractText
The TRAF-3 gene encodes a number of splice-variant isoforms that function as adapter molecules in NF-kappaB signaling, in part by associating with the cytoplasmic tails of CD40 or other TNF-receptor (TNF-R) family members. To identify downstream molecules in TRAF-3 signaling, a yeast two-hybrid library was screened with a full-length TRAF-3 construct. Nine independent TRAF-3 interacting clones encoded fragments of p62 Nucleoporin (p62), a 522 amino acid (aa) component of the nuclear pore central plug, that is known to bind karyopherin-beta/classical-NLS import factor complexes. The interaction of p62 with TRAF-3 was specific, since p62 failed to interact with TRAF-2, -4, -5, or -6. Deletional analysis in yeast revealed that the p62:TRAF-3 interaction is mediated by a p62 carboxy (C)-terminal coiled-coil domain and TRAF-3's fifth zinc (Zn) finger and coiled-coil domain. In human 293 T cells, recombinant TRAF-3 or p62 specifically co-immunoprecipitates the other species. In addition, endogenous p62 co-precipitates over-expressed TRAF-3. The functional effects of over-expressing a TRAF-3 binding fragment, p62(aa 336-522) were studied on NF-kappaB-dependent, or control STAT1-dependent reporter activity in 293 T cells, either resting or after stimulation by CD40 or IFN-gamma, respectively. Over-expression of p62(aa 336-522) induces NF-kappaB activation in resting cells and augments CD40-induced NF-kappaB activation, but has no effect on control STAT1 reporter activity, either at baseline or after IFN-gamma induction. The finding that TRAF-3 binds p62, suggests that TRAF-3 may serve as an adapter molecule at the nuclear membrane, in addition to its known adapter function at the plasma membrane.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD40, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STAT1 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/STAT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 3, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/beta Karyopherins, http://linkedlifedata.com/resource/pubmed/chemical/nuclear pore protein p62
pubmed:status
MEDLINE
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
73-84
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
TRAF-3 interacts with p62 nucleoporin, a component of the nuclear pore central plug that binds classical NLS-containing import complexes.
pubmed:affiliation
Laboratory of Molecular Immunology, Columbia University, New York, NY 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't