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http://purl.uniprot.org/citations/15885653http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15885653http://www.w3.org/2000/01/rdf-schema#comment"Here, we identify Cys351 and Cys361 as novel residues critical for the function and plasma membrane targeting of the Na+/glucose transporter-1 (SGLT1). HEK-293 cells expressing the C351A and C361A mutants showed no detectable Na(+)-coupled uptake for alpha-methyl glucoside (AMG). Cell-surface biotinylation and Western blot revealed that the two mutants were overexpressed in 293 cells; however, none of them exhibited normal cell-surface expression. When reconstituted in proteoliposomes, mutant SGLT1s demonstrated significantly lower affinity for AMG compared with the wild-type transporter. Incubation with the reducing agent dithiothreitol did not alter the catalytic activity of wild-type protein, but surprisingly, it nearly restored the ability of SGLT1-C351A and -C361A to bind and translocate AMG. Thus, the C351A and C361A mutations might cause a global reorganization of the disulfide bonds of SGLT1. Furthermore, we showed that a double mutation (C351A/C361A) restored the cell-surface expression of the single C-to-A mutants (C351A and C361A)."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2005.04.010"xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/author"Peng Y."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/author"Xia X."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/author"Jen J."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/name"Arch Biochem Biophys"xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/pages"63-69"xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/title"Cys351 and Cys361 of the Na+/glucose cotransporter are important for both function and cell-surface expression."xsd:string
http://purl.uniprot.org/citations/15885653http://purl.uniprot.org/core/volume"438"xsd:string
http://purl.uniprot.org/citations/15885653http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15885653
http://purl.uniprot.org/citations/15885653http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15885653
http://purl.uniprot.org/uniprot/#_P13866-mappedCitation-15885653http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15885653
http://purl.uniprot.org/uniprot/#_A4QPH0-mappedCitation-15885653http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15885653
http://purl.uniprot.org/uniprot/A4QPH0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15885653
http://purl.uniprot.org/uniprot/P13866http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15885653