http://purl.uniprot.org/citations/22797923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22797923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22797923 | http://www.w3.org/2000/01/rdf-schema#comment | "Here, we describe a phosphorylation-based reverse myristoyl switch for mammalian ZNRF2, and show that this E3 ubiquitin ligase and its sister protein ZNRF1 regulate the Na(+)/K(+) pump (Na(+)/K(+)ATPase). N-myristoylation localizes ZNRF1 and ZNRF2 to intracellular membranes and enhances their activity. However, when ZNRF2 is phosphorylated in response to agonists including insulin and growth factors, it binds to 14-3-3 and is released into the cytosol. On membranes, ZNRF1 and ZNRF2 interact with the Na(+)/K(+)ATPase α1 subunit via their UBZ domains, while their RING domains interact with E2 proteins, predominantly Ubc13 that, together with Uev1a, mediates formation of Lys63-ubiquitin linkages. ZNRF1 and ZNRF2 can ubiquitylate the cytoplasmic loop encompassing the nucleotide-binding and phosphorylation regions of the Na(+)/K(+)ATPase α1 subunit. Ouabain, a Na(+)/K(+)ATPase inhibitor and therapeutic cardiac glycoside, decreases ZNRF1 protein levels, whereas knockdown of ZNRF2 inhibits the ouabain-induced decrease of cell surface and total Na(+)/K(+)ATPase α1 levels. Thus, ZNRF1 and ZNRF2 are new players in regulation of the ubiquitous Na(+)/K(+)ATPase that is tuned to changing demands in many physiological contexts."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.110296"xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.110296"xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Toth R."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Toth R."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "MacKintosh C."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "MacKintosh C."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Campbell D.G."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Campbell D.G."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Prescott A.R."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Prescott A.R."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Hoxhaj G."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Hoxhaj G."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Najafov A."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/author | "Najafov A."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/pages | "4662-4675"xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/pages | "4662-4675"xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/title | "ZNRF2 is released from membranes by growth factors and, together with ZNRF1, regulates the Na+/K+ATPase."xsd:string |
http://purl.uniprot.org/citations/22797923 | http://purl.uniprot.org/core/title | "ZNRF2 is released from membranes by growth factors and, together with ZNRF1, regulates the Na+/K+ATPase."xsd:string |