The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.

@article{Pelletier2000TheHS,
  title={The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.},
  author={M. F. Pelletier and A. Marcil and G. S{\'e}vigny and C. Jakob and D. Tessier and E. Chevet and R. M{\'e}nard and J. Bergeron and D. Thomas},
  journal={Glycobiology},
  year={2000},
  volume={10 8},
  pages={
          815-27
        }
}
Glucosidase II is an ER heterodimeric enzyme that cleaves sequentially the two innermost alpha-1,3-linked glucose residues from N-linked oligosaccharides on nascent glycoproteins. This processing allows the binding and release of monoglucosylated (Glc(1)Man(9)GlcNAc(2)) glycoproteins with calnexin and calreticulin, the lectin-like chaperones of the endoplasmic reticulum. We have isolated two cDNA isoforms of the human alpha subunit (alpha1 and alpha2) differing by a 66 bp stretch, and a cDNA… Expand
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Genetic analysis of glucosidase II beta-subunit in trimming of high-mannose-type glycans.
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Processing enzyme glucosidase II: proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland.
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Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.
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Sugar-binding activity of the MRH domain in the ER alpha-glucosidase II beta subunit is important for efficient glucose trimming.
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Glucosidase II and MRH-domain containing proteins in the secretory pathway.
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Yeast GTB1 Encodes a Subunit of Glucosidase II Required for Glycoprotein Processing in the Endoplasmic Reticulum*
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Endoplasmic reticulum glucosidase II is inhibited by its end products.
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UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control.
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Purification and partial biochemical characterization of a membrane-bound type II-like α-glucosidase from the yeast morphotype of Sporothrix schenckii
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Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control
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References

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