The Coxsackievirus and Adenovirus Receptor (CAR) Forms a Complex with the PDZ Domain-containing Protein Ligand-of-Numb Protein-X (LNX)
| Autor: | Lennart Philipson, Momina Mirza, Per O. Ljungdahl, Ralf F. Pettersson, Elisabeth Raschperger, Kerstin Sollerbrant, Ulla Engström |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Coxsackie and Adenovirus Receptor-Like Membrane Protein
DNA Complementary Transcription Genetic Recombinant Fusion Proteins Ubiquitin-Protein Ligases Blotting Western PDZ domain Plasma protein binding Biology Transfection Biochemistry Cell Line Fungal Proteins Mice Protein structure Two-Hybrid System Techniques Animals Humans Binding site Fluorescent Antibody Technique Indirect Molecular Biology Gene Library Glutathione Transferase Binding Sites Virus receptor C-terminus Cell Biology Protein Structure Tertiary Cell biology Protein Biosynthesis NUMB Receptors Virus Carrier Proteins human activities Cell Division Plasmids Protein Binding Protein ligand |
| Zdroj: | Journal of Biological Chemistry. 278:7439-7444 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m205927200 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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