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The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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2003 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 278, no 9, 7439-7444 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2003. Vol. 278, no 9, 7439-7444 p.
Keyword [en]
Animals, Binding Sites, Blotting; Western, Carrier Proteins/*chemistry/metabolism, Cell Division, Cell Line, DNA; Complementary/metabolism, Fluorescent Antibody Technique; Indirect, Fungal Proteins/metabolism, Gene Library, Glutathione Transferase/metabolism, Humans, Mice, Plasmids/metabolism, Protein Binding, Protein Biosynthesis, Protein Structure; Tertiary, Receptors; Virus/*chemistry/*metabolism, Recombinant Fusion Proteins/metabolism, Transcription; Genetic, Transfection, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-10804DOI: 10.1074/jbc.M205927200PubMedID: 12468544OAI: oai:DiVA.org:uu-10804DiVA: diva2:38572
Available from: 2007-04-25 Created: 2007-04-25 Last updated: 2017-12-11Bibliographically approved

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Engström, UllaPhilipson, Lennart

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