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http://purl.uniprot.org/citations/15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15090548http://www.w3.org/2000/01/rdf-schema#comment"CHT1 is a Na(+)- and Cl(-)-dependent, hemicholinium-3 (HC-3)-sensitive, high affinity choline transporter. Par-4 (prostate apoptosis response-4) is a leucine zipper protein involved in neuronal degeneration and cholinergic signaling in Alzheimer's disease. We now report that Par-4 is a negative regulator of CHT1 choline uptake activity. Transfection of neural IMR-32 cells with human CHT1 conferred Na(+)-dependent, HC-3-sensitive choline uptake that was effectively inhibited by cotransfection of Par-4. Mapping studies indicated that the C-terminal half of Par-4 was physically involved in interacting with CHT1, and the absence of Par-4.CHT1 complex formation precluded the loss of CHT1-mediated choline uptake induced by Par-4, indicating that Par-4.CHT1 complex formation is essential. Kinetic and cell-surface biotinylation assays showed that Par-4 inhibited CHT1-mediated choline uptake by reducing CHT1 expression in the plasma membrane without significantly altering the affinity of CHT1 for choline or HC-3. These results suggest that Par-4 is directly involved in regulating choline uptake by interacting with CHT1 and by reducing its incorporation on the cell surface."xsd:string
http://purl.uniprot.org/citations/15090548http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m401495200"xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/author"Xie J."xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/author"Guo Q."xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/pages"28266-28275"xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/title"Par-4 inhibits choline uptake by interacting with CHT1 and reducing its incorporation on the plasma membrane."xsd:string
http://purl.uniprot.org/citations/15090548http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15090548http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15090548
http://purl.uniprot.org/citations/15090548http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15090548
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http://purl.uniprot.org/uniprot/#_B4DUU7-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
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http://purl.uniprot.org/uniprot/#_Q925B0-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
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http://purl.uniprot.org/uniprot/#_Q8BGY9-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
http://purl.uniprot.org/uniprot/#_Q3UWE8-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
http://purl.uniprot.org/uniprot/#_Q3TPV0-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
http://purl.uniprot.org/uniprot/#_Q96IZ0-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
http://purl.uniprot.org/uniprot/#_Q9GZV3-mappedCitation-15090548http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15090548
http://purl.uniprot.org/uniprot/Q925B0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15090548
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http://purl.uniprot.org/uniprot/Q3TPV0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15090548