PMID:18216284

Citation	Uccelletti, D, Pascoli, A, Farina, F, Alberti, A, Mancini, P, Hirschberg, CB and Palleschi, C (2008) APY-1, a novel Caenorhabditis elegans apyrase involved in unfolded protein response signalling and stress responses. Mol. Biol. Cell 19:1337-45
Abstract	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.
Links	PubMed PMC2291423 Online version:10.1091/mbc.E07-06-0547
Keywords	Animals; Animals, Genetically Modified; Apyrase/antagonists & inhibitors; Apyrase/genetics; Apyrase/metabolism; Base Sequence; Caenorhabditis elegans/genetics; Caenorhabditis elegans/growth & development; Caenorhabditis elegans/metabolism; Caenorhabditis elegans Proteins/chemistry; Caenorhabditis elegans Proteins/genetics; Caenorhabditis elegans Proteins/metabolism; DNA, Helminth/genetics; Endoplasmic Reticulum/metabolism; Gene Expression Regulation; Genes, Helminth; Glycosylation; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Mutation; Pharynx/enzymology; Pharynx/growth & development; Protein Folding; Pyrophosphatases/antagonists & inhibitors; Pyrophosphatases/genetics; Pyrophosphatases/metabolism; RNA Interference; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Signal Transduction
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