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The UDP-Glc:glycoprotein glucosyltransferase (UGGT) is the sensor of glycoprotein conformations in the glycoprotein folding quality control as it exclusively glucosylates glycoproteins not displaying their native conformations. Monoglucosylated glycoproteins thus formed may interact with the lectin-chaperones calnexin (CNX) and calreticulin (CRT). This interaction prevents premature exit of folding intermediates to the Golgi and enhances folding efficiency. Bioinformatic analysis showed that in  C. elegans  there are two open reading frames (F48E3.3 and F26H9.8 to be referred as  uggt-1  and  uggt-2 , respectively) coding for UGGT homologues. Expression of both genes in  Schizosaccharomyces pombe  mutants devoid of UGGT activity showed that  uggt-1  codes for an active UGGT protein (CeUGGT-1). On the other hand,  uggt-2  coded for a protein (CeUGGT-2) apparently not displaying a canonical UGGT activity. This protein was essential for viability, although cnx/crt null worms were viable. We constructed transgenic worms carrying the  uggt-1  promoter linked to the green fluorescent protein (GFP) coding sequence and found that CeUGGT-1 is expressed in cells of the nervous system.  uggt-1  is upregulated under ER stress through the  ire-1  arm of the unfolded protein response (UPR). Real-time PCR analysis showed that both  uggt-1  and  uggt-2  genes are expressed during the entire  C. elegans  life cycle. RNAi-mediated depletion of CeUGGT-1 but not of CeUGGT-2 resulted in a reduced lifespan and that of CeUGGT-1 and CeUGGT-2 in a developmental delay. We found that both CeUGGT1 and CeUGGT2 play a protective role under ER stress conditions, since 10 µg/ml tunicamycin arrested development at the L2/L3 stage of both  uggt-1(RNAi)  and  uggt-2(RNAi)  but not of control worms. Furthermore, we found that the role of CeUGGT-2 but not CeUGGT-1 is significant in relieving low ER stress levels in the absence of the  ire-1  unfolding protein response signaling pathway. Our results indicate that both  C. elegans  UGGT homologues have distinct biological functions.

The Two Caenorhabditis elegans UDP-Glucose:Glycoprotein Glucosyltransferase Homologues Have Distinct Biological Functions