The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX)

• 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.

Nyckelord

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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