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http://purl.uniprot.org/citations/21063096http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21063096http://www.w3.org/2000/01/rdf-schema#comment"The serum- and glucocorticoid-regulated kinase (Sgk1) is essential for hormonal regulation of ENaC-mediated sodium transport and is involved in the transduction of growth-factor-dependent cell survival and proliferation. The identification of molecular partners for Sgk1 is crucial for the understanding of its mechanisms of action. We performed a yeast two-hybrid screening based on a human kidney cDNA library to identify molecular partners of Sgk1. As a result the screening revealed a specific interaction between Sgk1 and a 60 kDa Lysophospholipase (LysoLP). LysoLP is a poorly characterized enzyme that, based on sequence analysis, might possess lysophospholipase and asparaginase activities. We demonstrate that LysoLP has indeed a lysophospholipase activity and affects metabolic functions related to cell proliferation and regulation of membrane channels. Moreover we demonstrate in the Xenopus oocyte expression system that LysoLP downregulates basal and Sgk1-dependent ENaC activity. In conclusion LysoLP may represent a new player in the regulation of ENaC and Sgk1-dependent signaling."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.org/dc/terms/identifier"doi:10.1159/000322326"xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Lang F."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Corda D."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Perrotti N."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Mariggio S."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Menniti M."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Iuliano R."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Nofziger C."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Amato R."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Alesutan I."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Sopjani M."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Foller M."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Blazer-Yost B."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/author"Perri A.M."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/name"Cell Physiol Biochem"xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/pages"587-596"xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/title"60kDa lysophospholipase, a new Sgk1 molecular partner involved in the regulation of ENaC."xsd:string
http://purl.uniprot.org/citations/21063096http://purl.uniprot.org/core/volume"26"xsd:string
http://purl.uniprot.org/citations/21063096http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21063096
http://purl.uniprot.org/citations/21063096http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21063096
http://purl.uniprot.org/uniprot/#_G3V1Y8-mappedCitation-21063096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21063096
http://purl.uniprot.org/uniprot/#_Q86U10-mappedCitation-21063096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21063096