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http://purl.uniprot.org/citations/24140420http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24140420http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24140420http://www.w3.org/2000/01/rdf-schema#comment"The selective degradation of intracellular components by autophagy involves sequential interactions of the cargo with a receptor, which also binds the autophagosomal protein Atg8 and a scaffold protein. Here, we demonstrated that mutations in C. elegans epg-11, which encodes an arginine methyltransferase homologous to PRMT1, cause the defective removal of PGL-1 and PGL-3 (cargo)-SEPA-1 (receptor) complexes, known as PGL granules, from somatic cells during embryogenesis. Autophagic degradation of the PGL granule scaffold protein EPG-2 and other protein aggregates was unaffected in epg-11/prmt-1 mutants. Loss of epg-11/prmt-1 activity impairs the association of PGL granules with EPG-2 and LGG-1 puncta. EPG-11/PRMT-1 directly methylates arginines in the RGG domains of PGL-1 and PGL-3. Autophagic removal of PGL proteins is impaired when the methylated arginines are mutated. Our study reveals that posttranslational arginine methylation regulates the association of the cargo-receptor complex with the scaffold protein, providing a mechanism for modulating degradation efficiency in selective autophagy."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2013.09.014"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2013.09.014"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Yang P."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Yang P."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Tian E."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/author"Tian E."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/pages"421-433"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/pages"421-433"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/title"Arginine methylation modulates autophagic degradation of PGL granules in C. elegans."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/title"Arginine methylation modulates autophagic degradation of PGL granules in C. elegans."xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/volume"52"xsd:string
http://purl.uniprot.org/citations/24140420http://purl.uniprot.org/core/volume"52"xsd:string
http://purl.uniprot.org/citations/24140420http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24140420
http://purl.uniprot.org/citations/24140420http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24140420