The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction
The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction
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DOI：
10.1074/jbc.m409061200
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发表时间：
2004-11-12
影响因子：
4.8
通讯作者：
Bergelson, JM
中科院分区：
文献类型：
--
作者：
Coyne, CB;Voelker, T;Bergelson, JM
柯萨奇病毒和腺病毒受体（CAR）是上皮细胞紧密连接的组成部分。在酵母双杂交筛选中，我们鉴定了多PDZ结构域蛋白MUPP 1作为CAR胞质结构域的相互作用伴侣。发现CAR和MUPP 1共定位于紧密连接处，从上皮细胞共沉淀，并在体外相互作用。发现该相互作用特异性涉及CAR C末端和MUPP 1 PDZ结构域13内的PDZ结合基序。在转染的细胞中，CAR募集MUPP 1进行细胞-细胞接触。用小干扰RNA抑制CAR表达抑制了MUPP 1定位于紧密连接。结果表明，CAR与MUPP 1相互作用，并参与MUPP 1向紧密连接的募集。
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.