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http://purl.uniprot.org/citations/18216284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18216284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18216284http://www.w3.org/2000/01/rdf-schema#comment"Protein glycosylation modulates a wide variety of intracellular events and dysfunction of the glycosylation pathway has been reported in a variety of human pathologies. Endo-apyrases have been suggested to have critical roles in protein glycosylation and sugar metabolism. However, deciphering the physiological relevance of Endo-apyrases activity has actually proved difficult, owing to their complexity and the functional redundancy within the family. We report here that a UDP/GDPase, homologous to the human apyrase Scan-1, is present in the membranes of Caenorhabditis elegans, encoded by the ORF F08C6.6 and hereinafter-named APY-1. We showed that ER stress induced by tunicamycin or high temperature resulted in increased transcription of apy-1. This increase was not observed in C. elegans mutants defective in ire-1 or atf-6, demonstrating the requirement of both ER stress sensors for up-regulation of apy-1. Depletion of APY-1 resulted in constitutively activated unfolded protein response. Defects in the pharynx and impaired organization of thin fibers in muscle cells were observed in adult worms depleted of APY-1. Some of the apy-1(RNAi) phenotypes are suggestive of premature aging, because these animals also showed accumulation of lipofuscin and reduced lifespan that was not dependent on the functioning of DAF-2, the receptor of the insulin/IGF-1 signaling pathway."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e07-06-0547"xsd:string
http://purl.uniprot.org/citations/18216284http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e07-06-0547"xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Alberti A."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Alberti A."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Mancini P."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Mancini P."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Farina F."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Farina F."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Hirschberg C.B."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Hirschberg C.B."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Palleschi C."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Palleschi C."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Pascoli A."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Pascoli A."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Uccelletti D."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/author"Uccelletti D."xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/pages"1337-1345"xsd:string
http://purl.uniprot.org/citations/18216284http://purl.uniprot.org/core/pages"1337-1345"xsd:string