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http://purl.uniprot.org/citations/12444018http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12444018http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12444018http://www.w3.org/2000/01/rdf-schema#comment"The electroneutral sodium bicarbonate cotransporter 3 (NBC3) coimmunoprecipitates from renal lysates with the vacuolar H(+)-ATPase. In renal type A and B intercalated cells, NBC3 colocalizes with the vacuolar H(+)-ATPase. The involvement of the COOH termini of NBC3 and the 56-kDa subunit of the proton pump in the interaction of these proteins was investigated. The intact and modified COOH termini of NBC3 and the 56-kDa subunit of the proton pump were synthesized, coupled to Sepharose beads, and used to pull down kidney membrane proteins. Both the 56- and the 70-kDa subunits of the proton pump, as well as a PDZ domain containing protein Na(+)/H(+) exchanger regulatory factor 1 (NHERF-1), were bound to the intact 18 amino acid NBC3 COOH terminus. A peptide truncated by five COOH-terminal amino acids did not bind these proteins. Replacement of the COOH-terminal leucine with glycine blocked binding of both the proton pump subunits but did not affect binding of NHERF-1. The 18 amino acid COOH terminus of the 56-kDa subunit of the proton pump bound NHERF-1 and NBC3, but the truncated and modified peptide did not. A complex of NBC3, the 56-kDa subunit of the proton pump, and NHERF-1 was identified in rat kidney. The data indicate that the COOH termini of NBC3 and the 56-kDa subunit of the vacuolar proton pump are PDZ-interacting motifs that are necessary for the interaction of these proteins. NHERF-1 is involved in the interaction of NBC3 and the vacuolar proton pump."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.org/dc/terms/identifier"doi:10.1152/ajpcell.00225.2002"xsd:string
http://purl.uniprot.org/citations/12444018http://purl.org/dc/terms/identifier"doi:10.1152/ajpcell.00225.2002"xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Newman D."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Newman D."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Abuladze N."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Abuladze N."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Kurtz I."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Kurtz I."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Pushkin A."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Pushkin A."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Sassani P."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Sassani P."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Tatishchev S."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Tatishchev S."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Muronets V."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/author"Muronets V."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/pages"C667-C673"xsd:string
http://purl.uniprot.org/citations/12444018http://purl.uniprot.org/core/pages"C667-C673"xsd:string