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http://purl.uniprot.org/citations/27613864http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27613864http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27613864http://www.w3.org/2000/01/rdf-schema#comment"Progressive rod-cone degeneration (PRCD) is a photoreceptor outer segment (OS) disc-specific protein with unknown function that is associated with retinitis pigmentosa (RP). The most common mutation in PRCD linked with severe RP phenotype is substitution of the only cysteine to tyrosine (C2Y). In this study, we find that PRCD is post-translationally modified by a palmitoyl lipid group at the cysteine residue linked with RP. Disrupting PRCD palmitoylation either chemically or by genetically eliminating the modified cysteine dramatically affects the stability of PRCD. Furthermore, in vivo electroporation of PRCD C2Y mutant in the mouse retina demonstrates that the palmitoylation of PRCD is important for its proper localization in the photoreceptor OS. Mutant PRCD C2Y was found in the inner segment in contrast to normal localization of WT PRCD in the OS. Our results also suggest that zDHHC3, a palmitoyl acyltransferase (PAT), catalyzes the palmitoylation of PRCD in the Golgi compartment. In conclusion, we find that the palmitoylation of PRCD is crucial for its trafficking to the photoreceptor OS and mislocalization of this protein likely leads to RP-related phenotypes."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.742767"xsd:string
http://purl.uniprot.org/citations/27613864http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.742767"xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/author"Murphy J."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/author"Murphy J."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/author"Kolandaivelu S."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/author"Kolandaivelu S."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/pages"23036-23046"xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/pages"23036-23046"xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/title"Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates Protein Stability and Localization."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/title"Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates Protein Stability and Localization."xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/volume"291"xsd:string
http://purl.uniprot.org/citations/27613864http://purl.uniprot.org/core/volume"291"xsd:string
http://purl.uniprot.org/citations/27613864http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27613864
http://purl.uniprot.org/citations/27613864http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27613864
http://purl.uniprot.org/citations/27613864http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27613864
http://purl.uniprot.org/citations/27613864http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27613864
http://purl.uniprot.org/uniprot/Q00LT2http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27613864
http://purl.uniprot.org/uniprot/Q8R173http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27613864