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Originally published In Press as doi:10.1074/jbc.M409061200 on September 9, 2004

J. Biol. Chem., Vol. 279, Issue 46, 48079-48084, November 12, 2004
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The Coxsackievirus and Adenovirus Receptor Interacts with the Multi-PDZ Domain Protein-1 (MUPP-1) within the Tight Junction*

Carolyn B. Coyne, Tauni Voelker, Susan L. Pichla, and Jeffrey M. Bergelson{ddagger}

From the Division of Infectious Diseases, Children's Hospital of Philadelphia, Pennsylvania 19104

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.


Received for publication, August 9, 2004 , and in revised form, September 8, 2004.

* This work was supported by Grants R01AI5228-1, R01HL54734, and T32AI07324 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: 1202 Abramson Research Center, Children's Hospital of Philadelphia, 3615 Civic Center Blvd., Philadelphia, PA 19104. Tel.: 215-590-3771; Fax: 215-590-2025; E-mail: bergelson{at}email.chop.edu.


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