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

被引:81
作者
Sollerbrant, K
Raschperger, E
Mirza, M
Engström, U
Philipson, L
Ljungdahl, PO
Pettersson, RF
机构
[1] Karolinska Inst, Stockholm Branch, Ludwig Inst Canc Res, SE-17177 Stockholm, Sweden
[2] Ludwig Inst Canc Res, Uppsala Branch, SE-75124 Uppsala, Sweden
[3] Karolinska Inst, Dept Cell & Mol Biol, SE-17177 Stockholm, Sweden
关键词
D O I
10.1074/jbc.M205927200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页码:7439 / 7444
页数:6
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