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rdf:type |
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lifeskim:mentions |
umls-concept:C0004381,
umls-concept:C0007577,
umls-concept:C0010243,
umls-concept:C0018270,
umls-concept:C0035820,
umls-concept:C0250783,
umls-concept:C1413828,
umls-concept:C1417827,
umls-concept:C1420354,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
Pt 19
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pubmed:dateCreated |
2004-8-27
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pubmed:abstractText |
The coxsackie and adenovirus receptor (CAR) plays a role in viral infection, maintenance of the junction adhesion complex in polarized epithelia, and modulation of cellular growth properties. As a viral receptor, the C-terminus appears to play no role indicating that the major function of CAR is to tether the virus to the cell. By contrast, the C-terminus is known to play a role in cellular localization and probably has a significant function in CAR-mediated adhesion and cell growth properties. We hypothesized that the CAR PDZ (PSD-95/Disc-large/ZO-1) binding motif interacts with PDZ-domain-containing proteins to modulate the cellular phenotype. CAR was modified by deleting the last four amino acids (CARDeltaGSIV) and evaluated for cell-cell adhesion in polarized primary human airway epithelia and growth characteristics in stably transfected L-cells. Although ablation of the CAR PDZ-binding motif did not affect adenoviral infection, it did have a significant effect both on cell-cell adhesion and on cell growth. Expression of CARDeltaGSIV failed to increase the transepithelial resistance in polarized epithelia to the same degree as wild-type CAR and failed to act as a growth modulator in L-cells. Furthermore, we provide evidence for three new CAR interacting partners, including MAGI-1b, PICK1 and PSD-95. CAR appears to interact with several distinct PDZ-domain-containing proteins and may exert its biological function through these interactions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CXADR-like membrane protein,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dlgh4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PICk1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Prkcabp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4401-9
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15304526-Animals,
pubmed-meshheading:15304526-COS Cells,
pubmed-meshheading:15304526-Carrier Proteins,
pubmed-meshheading:15304526-Cell Adhesion,
pubmed-meshheading:15304526-Cell Proliferation,
pubmed-meshheading:15304526-Cercopithecus aethiops,
pubmed-meshheading:15304526-Electric Impedance,
pubmed-meshheading:15304526-Epithelial Cells,
pubmed-meshheading:15304526-Guanylate Kinase,
pubmed-meshheading:15304526-Humans,
pubmed-meshheading:15304526-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15304526-L Cells (Cell Line),
pubmed-meshheading:15304526-Lung,
pubmed-meshheading:15304526-Membrane Proteins,
pubmed-meshheading:15304526-Mice,
pubmed-meshheading:15304526-Mutation,
pubmed-meshheading:15304526-Nerve Tissue Proteins,
pubmed-meshheading:15304526-Nuclear Proteins,
pubmed-meshheading:15304526-Protein Structure, Tertiary,
pubmed-meshheading:15304526-Receptors, Virus
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pubmed:year |
2004
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pubmed:articleTitle |
A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth.
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pubmed:affiliation |
Department of Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 200 Hawkins Drive, Iowa City, IA 52242, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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