http://purl.uniprot.org/citations/15699339 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15699339 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15699339 | http://www.w3.org/2000/01/rdf-schema#comment | "The neuronal Na(+)/H(+) exchanger NHE5 isoform not only resides in the plasma membrane but also accumulates in recycling vesicles by means of clathrin-mediated endocytosis. To further investigate the underlying molecular mechanisms, a human brain cDNA library was screened for proteins that interact with the cytoplasmic C-terminal region of NHE5 by using yeast two-hybrid methodology. One candidate cDNA identified by this procedure encoded beta-arrestin2, a specialized adaptor/scaffolding protein required for internalization and signaling of members of the G protein-coupled receptor superfamily. Direct interaction between the two proteins was demonstrated in vitro by GST fusion protein pull-down assays. Sequences within the N-terminal receptor activation-recognition domain and the C-terminal secondary receptor-binding domain of beta-arrestin2 conferred strong binding to the C terminus of NHE5. Full-length NHE5 and beta-arrestin2 also associated in intact cells, as revealed by their coimmunoprecipitation from extracts of transfected CHO cells. Moreover, ectopic expression of both proteins caused a redistribution of beta-arrestin2 from the cytoplasm to vesicles containing NHE5, and significantly decreased the abundance of the transporter at the cell surface. Comparable results were also obtained for the beta-arrestin1 isoform. These data reveal a broader role for arrestins in the trafficking of integral plasma membrane proteins than previously recognized."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0407444102"xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0407444102"xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Orlowski J."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Orlowski J."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Iannuzzi P."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Iannuzzi P."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Lukashova V."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Lukashova V."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Numata M."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Numata M."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Szabo E.Z."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/author | "Szabo E.Z."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/pages | "2790-2795"xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/pages | "2790-2795"xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/title | "beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/title | "beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform."xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/volume | "102"xsd:string |
http://purl.uniprot.org/citations/15699339 | http://purl.uniprot.org/core/volume | "102"xsd:string |