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Papers In Press, published online ahead of print January 31, 2001
J. Biol. Chem, 10.1074/jbc.C100023200
Submitted on January 17, 2001
Revised on January 31, 2001
Accepted on January 31, 2001
-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for ER associated degradation of glycoproteins
Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya, Aichi-ken 464-8602
Corresponding Author: endo{at}biochem.chem.nagoya-u.ac.jp
The endoplasmic reticulum (ER) has a mechanism to block the exit of misfolded or unassembled proteins from the ER for the downstream organelles in the secretory pathway. Misfolded proteins retained in the ER are subjected to proteasome-dependent degradation in the cytosol when they cannot achieve correct folding and/or assembly within an appropriate time window. Although specific mannose trimming of the protein-bound oligosaccharide is essential for the degradation of misfolded glycoproteins, the precise mechanism for this recognition remains obscure. Here we report a new 
-mannosidase-like protein, Mnl1p (mannosidase-like protein), in the yeast ER. Mnl1p is unlikely to exhibit 1,2-mannosidase activity because it lacks cystein residues that are essential for 1,2-mannosidase. However deletion of the MNL1 gene causes retardation of the degradation of misfolded carboxypeptidase Y, but not of the unglycosylated mutant form of the yeast -mating pheromone. Possible roles of Mnl1p in the degradation and in the ER-retention of misfolded glycoproteins are discussed.
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