Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Biomarkers
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CHO Cells
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Caco-2 Cells
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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Cricetinae
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Endosomes / metabolism
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Epithelial Cells / cytology
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Epithelial Cells / metabolism
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Humans
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Membrane Proteins
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Protein Structure, Tertiary
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RNA, Small Interfering / genetics
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RNA, Small Interfering / metabolism
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Receptors, Virus / chemistry
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Receptors, Virus / genetics
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Receptors, Virus / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Tight Junctions / chemistry
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Tight Junctions / metabolism*
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Two-Hybrid System Techniques
Substances
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Biomarkers
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CLMP protein, human
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Carrier Proteins
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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MPDZ protein, human
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Membrane Proteins
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RNA, Small Interfering
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Receptors, Virus
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Recombinant Fusion Proteins