Coyne Carolyn B, Voelker Tauni, Pichla Susan L, Bergelson Jeffrey M
Division of Infectious Diseases, Children's Hospital of Philadelphia, Pennsylvania 19104, USA.
J Biol Chem. 2004 Nov 12;279(46):48079-84. doi: 10.1074/jbc.M409061200. Epub 2004 Sep 9.
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.
柯萨奇病毒和腺病毒受体（CAR）是上皮细胞紧密连接的一个组成部分。在酵母双杂交筛选中，我们鉴定出多PDZ结构域蛋白MUPP1是CAR细胞质结构域的相互作用伴侣。发现CAR和MUPP1共定位于紧密连接，可从上皮细胞中共沉淀，并在体外相互作用。发现这种相互作用特别涉及CAR C末端的PDZ结合基序和MUPP1的PDZ结构域13。在转染细胞中，CAR将MUPP1募集到细胞间接触部位。用小干扰RNA抑制CAR表达可抑制MUPP1定位于紧密连接。结果表明，CAR与MUPP1相互作用，并参与MUPP1募集到紧密连接的过程。
