Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 46, Pages 48079-48084Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M409061200
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Funding
- NHLBI NIH HHS [R01HL54734] Funding Source: Medline
- NIAID NIH HHS [T32AI07324, R01AI5228-1] Funding Source: Medline
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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.
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