The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction

被引：107

作者：

Coyne, CB ^{[1
]}

Voelker, T ^{[1
]}

Pichla, SL ^{[1
]}

Bergelson, JM ^{[1
]}

机构：

[1] Childrens Hosp Philadelphia, Div Infect Dis, Abramson Res Ctr 1202, Philadelphia, PA 19104 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2004年 / 279卷 / 46期

关键词：

D O I：

10.1074/jbc.M409061200

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) is a component of the epithelial cell tight junction. In a yeast two-hybrid screen we identified the multi-PDZ domain protein MUPP1 as an interaction partner for the CAR cytoplasmic domain. CAR and MUPP1 were found to colocalize at the tight junction, to coprecipitate from epithelial cells, and to interact in vitro. The interaction was found to specifically involve the PDZ-binding motif within the CAR C terminus and MUPP1 PDZ domain 13. In transfected cells, CAR recruited MUPP1 to cell-cell contacts. The inhibition of CAR expression with small interfering RNA inhibited MUPP1 localization to the tight junction. The results indicated that CAR interacts with MUPP1 and is involved in MUPP1 recruitment to the tight junction.

引用

页码：48079 / 48084

页数：6

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