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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2003-2-24
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pubmed:abstractText |
The Coxsackievirus and adenovirus receptor (CAR) functions as a virus receptor, but its primary biological function is unknown. A yeast two-hybrid screen was used to identify Ligand-of-Numb protein-X (LNX) as a binding partner to the intracellular tail of CAR. LNX harbors several protein-protein interacting domains, including four PDZ domains, and was previously shown to bind to and regulate the expression level of the cell-fate determinant Numb. CAR was able to bind LNX both in vivo and in vitro. Efficient binding to LNX required not only the consensus PDZ domain binding motif in the C terminus of CAR but also upstream sequences. The CAR binding region in LNX was mapped to the second PDZ domain. CAR and LNX were also shown to colocalize in vivo in mammalian cells. We speculate that CAR and LNX are part of a larger protein complex that might have important functions at discrete subcellular localizations in the cell.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CXADR-like membrane protein,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/LNX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lnx1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7439-44
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pubmed:dateRevised |
2011-7-1
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pubmed:meshHeading |
pubmed-meshheading:12468544-Animals,
pubmed-meshheading:12468544-Binding Sites,
pubmed-meshheading:12468544-Blotting, Western,
pubmed-meshheading:12468544-Carrier Proteins,
pubmed-meshheading:12468544-Cell Division,
pubmed-meshheading:12468544-Cell Line,
pubmed-meshheading:12468544-DNA, Complementary,
pubmed-meshheading:12468544-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:12468544-Fungal Proteins,
pubmed-meshheading:12468544-Gene Library,
pubmed-meshheading:12468544-Glutathione Transferase,
pubmed-meshheading:12468544-Humans,
pubmed-meshheading:12468544-Mice,
pubmed-meshheading:12468544-Plasmids,
pubmed-meshheading:12468544-Protein Binding,
pubmed-meshheading:12468544-Protein Biosynthesis,
pubmed-meshheading:12468544-Protein Structure, Tertiary,
pubmed-meshheading:12468544-Receptors, Virus,
pubmed-meshheading:12468544-Recombinant Fusion Proteins,
pubmed-meshheading:12468544-Transcription, Genetic,
pubmed-meshheading:12468544-Transfection,
pubmed-meshheading:12468544-Two-Hybrid System Techniques,
pubmed-meshheading:12468544-Ubiquitin-Protein Ligases
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pubmed:year |
2003
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pubmed:articleTitle |
The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX).
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pubmed:affiliation |
Ludwig Institute for Cancer Research, Stockholm Branch, Karolinska Intitutet, SE-17177 Stockholm, Sweden. kerstin.sollerbrant@licr.ki.se
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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