QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 19, Issue 4, 1337-1345, April 2008

This Article Full Text Full Text (PDF) Supplemental Materials All Versions of this Article: E07-06-0547v1 19/4/1337    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Uccelletti, D. Articles by Palleschi, C. Search for Related Content PubMed PubMed Citation Articles by Uccelletti, D. Articles by Palleschi, C.

APY-1, a Novel Caenorhabditis elegans Apyrase Involved in Unfolded Protein Response Signalling and Stress Responses

D. Uccelletti^*, A. Pascoli^*, F. Farina, A. Alberti, P. Mancini, C. B. Hirschberg^||, and C. Palleschi^*

*Department of Developmental and Cell Biology, University of Rome "La Sapienza," 00185 Rome, Italy; Institut de Génétique et Microbiologie, UMR8621, Université Paris-Sud, 91405 Orsay Cedex, France; Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique UPR 2167, 91198 Gif-sur-Yvette Cedex, France; Department of Experimental Medicine and Pathology, University of Rome "La Sapienza, 00161 Rome Italy; and ^||Department of Molecular and Cell Biology, Goldman School of Dental Medicine, Boston University, Boston, MA 02215

Submitted June 8, 2007; Revised January 4, 2008; Accepted January 10, 2008
Monitoring Editor: Benjamin Glick

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.

Address correspondence to: Daniela Uccelletti (daniela.uccelletti{at}uniroma1.it).

This article has been cited by other articles:

				K. Dejima, D. Murata, S. Mizuguchi, K. H. Nomura, K. Gengyo-Ando, S. Mitani, S. Kamiyama, S. Nishihara, and K. Nomura The ortholog of human solute carrier family 35 member B1 (UDP-galactose transporter-related protein 1) is involved in maintenance of ER homeostasis and essential for larval development in Caenorhabditis elegans FASEB J, July 1, 2009; 23(7): 2215 - 2225. [Abstract] [Full Text] [PDF]