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http://purl.uniprot.org/citations/22728137http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22728137http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22728137http://www.w3.org/2000/01/rdf-schema#comment"Gp78 is an E3 ubiquitin ligase within the endoplasmic reticulum-associated degradation pathway. We show that Flag-tagged gp78 undergoes sulfhydryl cysteine palmitoylation (S-palmitoylation) within the RING finger motif, responsible for its ubiquitin ligase activity. Screening of 19 palmitoyl acyl transferases (PATs) identified five that increased gp78 RING finger palmitoylation. Endoplasmic reticulum (ER)-localized Myc-DHHC6 overexpression promoted the peripheral ER distribution of Flag-gp78 while RING finger mutation and the palmitoylation inhibitor 2-bromopalmitate restricted gp78 to the central ER. Palmitoylation of RING finger cysteines therefore regulates gp78 distribution to the peripheral ER."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2012.06.011"xsd:string
http://purl.uniprot.org/citations/22728137http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2012.06.011"xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Huang K."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Huang K."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Nabi I.R."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Nabi I.R."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"El-Husseini A."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"El-Husseini A."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Fairbank M."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/author"Fairbank M."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/pages"2488-2493"xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/pages"2488-2493"xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/title"RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/title"RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase."xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/volume"586"xsd:string
http://purl.uniprot.org/citations/22728137http://purl.uniprot.org/core/volume"586"xsd:string
http://purl.uniprot.org/citations/22728137http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22728137
http://purl.uniprot.org/citations/22728137http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22728137