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http://purl.uniprot.org/citations/9295322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9295322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9295322http://www.w3.org/2000/01/rdf-schema#comment"Agonist-dependent internalization of the rat somatostatin receptor subtype 3 (SSTR3) requires four hydroxyl amino acids (Ser341, Ser346, Ser351, and Thr357) in the receptor C terminus (Roth, A., Kreienkamp, H.-J., Nehring, R., Roostermann, D., Meyerhof, W. and Richter, D. (1997) DNA Cell Biol. 16, 111-119). Here we report on the molecular mechanism responsible for the endocytotic process by analyzing the agonist-dependent phosphorylation of wild-type and mutant receptors expressed in human embryonic kidney cells. Wild-type SSTR3 is phosphorylated in response to agonist treatment. Phosphorylation is markedly reduced in a S341A/S346A/S351A triple mutant and is also reduced, but to a lesser extent, in the T357A point mutant. Internalization of the wild-type receptor is preceded by a functional desensitization of the receptor; in contrast, the triple serine mutant does not desensitize after treatment with agonists as assayed by its ability to inhibit forskolin-stimulated adenylate cyclase activity. After internalization via a clathrin-coated vesicle mediated endocytotic pathway, SSTR3 efficiently recycles to the cell surface, suggesting that agonist mediated endocytosis is necessary for the functional resensitization of a phosphorylated and desensitized receptor."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.38.23769"xsd:string
http://purl.uniprot.org/citations/9295322http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.38.23769"xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Richter D."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Richter D."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Meyerhof W."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Meyerhof W."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Roth A."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Roth A."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Kreienkamp H.-J."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/author"Kreienkamp H.-J."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/pages"23769-23774"xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/pages"23769-23774"xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/title"Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and internalization."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/title"Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and internalization."xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9295322http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9295322http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9295322
http://purl.uniprot.org/citations/9295322http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9295322