RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21847096http://www.w3.org/2000/01/rdf-schema#comment"ADAR2 catalyses the deamination of adenosine to inosine at the GluR2 Q/R site in the pre-mRNA encoding the critical subunit of AMPA receptors. Among ADAR2 substrates this is the vital one as editing at this position is indispensable for normal brain function. However, the regulation of ADAR2 post-translationally remains to be elucidated. We demonstrate that the phosphorylation-dependent prolyl-isomerase Pin1 interacts with ADAR2 and is a positive regulator required for the nuclear localization and stability of ADAR2. Pin1(-/-) mouse embryonic fibroblasts show mislocalization of ADAR2 in the cytoplasm and reduced editing at the GluR2 Q/R and R/G sites. The E3 ubiquitin ligase WWP2 plays a negative role by binding to ADAR2 and catalysing its ubiquitination and subsequent degradation. Therefore, ADAR2 protein levels and catalytic activity are coordinately regulated in a positive manner by Pin1 and negatively by WWP2 and this may have downstream effects on the function of GluR2. Pin1 and WWP2 also regulate the large subunit of RNA Pol II, so these proteins may also coordinately regulate other key cellular proteins."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.303"xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Hempel S."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Morrice N."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Brindle J."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Keegan L.P."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"O'Connell M.A."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Del Sal G."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Bisso A."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Paro S."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Casadio A."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/author"Marcucci R."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/pages"4211-4222"xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/title"Pin1 and WWP2 regulate GluR2 Q/R site RNA editing by ADAR2 with opposing effects."xsd:string
http://purl.uniprot.org/citations/21847096http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/21847096http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21847096
http://purl.uniprot.org/citations/21847096http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21847096
http://purl.uniprot.org/uniprot/#_A0A0A6YW90-mappedCitation-21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21847096
http://purl.uniprot.org/uniprot/#_A0A1D5RLH0-mappedCitation-21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21847096
http://purl.uniprot.org/uniprot/#_A0A1D5RM92-mappedCitation-21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21847096
http://purl.uniprot.org/uniprot/#_D6RDS5-mappedCitation-21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21847096
http://purl.uniprot.org/uniprot/#_P78563-mappedCitation-21847096http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21847096