Skip to main content
SpringerLink
Log in

Glucosidase, Alpha Neutral AB; Glucosidase II Subunit Beta (GANAB, PRKCSH, α-Glucosidase II)

  • Reference work entry
  • First Online:
Handbook of Glycosyltransferases and Related Genes

Abstract

The synthesis of N-linked glycans is initiated by the synthesis of a Glc3Man9GlcNAc2 lipid-linked precursor and the co-translational transfer to nascent polypeptide chains in the lumen of the endoplasmic reticulum (ER) (Kornfeld and Kornfeld 1985). Immediately after transfer of the glycan to Asn side chains glucose (Glc), trimming is initiated by the cleavage of the terminal α1,2-Glc residue by α-glucosidase I (MOGS). Subsequent cleavage of the two internal α1,3-Glc residues is accomplished by the heterodimeric enzyme α-glucosidase II (GANAB/PRKCSH) (Burns and Touster 1982; Grinna and Robbins 1979, 1980) to produce the Man9GlcNAc2-Asn processing intermediate (Fig. 114.1).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 799.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 549.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Alonso JM, Santa-Cecilia A, Calvo P (1991) Glucosidase II from rat liver microsomes. Kinetic model for binding and hydrolysis. Biochem J 278:721–727

    CAS  PubMed  Google Scholar 

  • Arendt CW, Ostergaard HL (1997) Identification of the CD45-associated 116-kDa and 80-kDa proteins as the α- and β-subunits of α-glucosidase II. J Biol Chem 272:13117–13125

    Article  CAS  PubMed  Google Scholar 

  • Arendt CW, Ostergaard HL (2000) Two distinct domains of the β-subunit of glucosidase II interact with the catalytic α-subunit. Glycobiology 10:487–492

    Article  CAS  PubMed  Google Scholar 

  • Arendt CW, Dawicki W, Ostergaard HL (1999) Alternative splicing of transcripts encoding the α- and β-subunits of mouse glucosidase II in T lymphocytes. Glycobiology 9:277–283

    Article  CAS  PubMed  Google Scholar 

  • Brada D, Dubach UC (1984) Isolation of a homogeneous glucosidase II from pig kidney microsomes. Eur J Biochem 141:149–156

    Article  CAS  PubMed  Google Scholar 

  • Brada D, Kerjaschki D, Roth J (1990) Cell type-specific post-Golgi apparatus localization of a “resident” endoplasmic reticulum glycoprotein, glucosidase II. J Cell Biol 110:309–318

    Article  CAS  PubMed  Google Scholar 

  • Burns DM, Touster O (1982) Purification and characterization of glucosidase II, an endoplasmic reticulum hydrolase involved in glycoprotein biosynthesis. J Biol Chem 257:9990–10000

    CAS  PubMed  Google Scholar 

  • Chiu CC, Lin CY, Lee LY, Chen YJ, Lu YC, Wang HM, Liao CT, Chang JT, Cheng AJ (2011) Molecular chaperones as a common set of proteins that regulate the invasion phenotype of head and neck cancer. Clin Cancer Res 17:4629–4641

    Article  CAS  PubMed  Google Scholar 

  • Datema R, Romero PA, Legler G, Schwarz RT (1982) Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol. Proc Natl Acad Sci USA 79:6787–6791

    Article  CAS  PubMed  Google Scholar 

  • Deprez P, Gautschi M, Helenius A (2005) More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell 19:183–195

    Article  CAS  PubMed  Google Scholar 

  • Fedeles SV, Tian X, Gallagher AR, Mitobe M, Nishio S, Lee SH, Cai Y, Geng L, Crews CM, Somlo S (2013) A genetic interaction network of five genes for human polycystic kidney and liver diseases defines polycystin-1 as the central determinant of cyst formation. Nat Genet 43:639–647

    Article  Google Scholar 

  • Feng J, Romaniouk AV, Samal SK, Vijay IK (2004) Processing enzyme glucosidase II: proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland. Glycobiology 14:909–921

    Article  CAS  PubMed  Google Scholar 

  • Flura T, Brada D, Ziak M, Roth J (1997) Expression of a cDNA encoding the glucose trimming enzyme glucosidase II in CHO cells and molecular characterization of the enzyme deficiency in a mutant mouse lymphoma cell line. Glycobiology 7:617–624

    Article  CAS  PubMed  Google Scholar 

  • Ganan S, Cazzulo JJ, Parodi AJ (1991) A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum. Biochemistry 30:3098–3104

    Article  CAS  PubMed  Google Scholar 

  • Grinna LS, Robbins PW (1979) Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J Biol Chem 254:8814–8818

    CAS  PubMed  Google Scholar 

  • Grinna LS, Robbins PW (1980) Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J Biol Chem 255:2255–2258

    CAS  PubMed  Google Scholar 

  • Hammond C, Helenius A (1995) Quality control in the secretory pathway. Curr Opin Cell Biol 7:523–529

    Article  CAS  PubMed  Google Scholar 

  • Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293:781–788

    CAS  PubMed  Google Scholar 

  • Henrissat B, Davies G (1997) Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 7:637–644

    Article  CAS  PubMed  Google Scholar 

  • Henrissat B, Romeu A (1995) Families, superfamilies and subfamilies of glycosyl hydrolases. Biochem J 311:350–351

    CAS  PubMed  Google Scholar 

  • Hentges A, Bause E (1997) Affinity purification and characterization of glucosidase II from pig liver. Biol Chem 378:1031–1038

    Article  CAS  PubMed  Google Scholar 

  • Hettkamp H, Bause E, Legler G (1982) Inhibition by nojirimycin and 1-deoxynojirimycin of microsomal glucosidases from calf liver acting on the glycoprotein oligosaccharides Glc1-3Man9GlcNAc2. Biosci Rep 2:899–906

    Article  CAS  PubMed  Google Scholar 

  • Hino Y, Rothman JE (1985) Glucosidase II, a glycoprotein of the endoplasmic reticulum membrane. Proteolytic cleavage into enzymatically active fragments. Biochemistry 24:800–805

    Article  CAS  PubMed  Google Scholar 

  • Hirai M, Shimizu N (1990) Purification of two distinct proteins of approximate Mr 80,000 from human epithelial cells and identification as proper substrates for protein kinase C. Biochem J 270:583–589

    CAS  PubMed  Google Scholar 

  • Hirano K, Ziak M, Kamoshita K, Sukenaga Y, Kametani S, Shiga Y, Roth J, Akanuma H (2000) N-linked oligosaccharide processing enzyme glucosidase II produces 1,5-anhydrofructose as a side product. Glycobiology 10:1283–1289

    Article  CAS  PubMed  Google Scholar 

  • Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631–664

    Article  CAS  PubMed  Google Scholar 

  • Li A, Davila S, Furu L, Qian Q, Tian X, Kamath PS, King BF, Torres VE, Somlo S (2003) Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease. Am J Hum Genet 72:691–703

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Martiniuk F, Ellenbogen A, Hirschhorn R (1985) Identity of neutral α-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies. J Biol Chem 260:1238–1242

    CAS  PubMed  Google Scholar 

  • Michael JM, Kornfeld S (1980) Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch Biochem Biophys 199:249–258

    Article  CAS  PubMed  Google Scholar 

  • Munro S (2001) The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr Biol 11:R499–R501

    Article  CAS  PubMed  Google Scholar 

  • Olson LJ, Orsi R, Alculumbre SG, Peterson FC, Stigliano ID, Parodi A, D’Alessio C, Dahms NM (2013) Structure of the lectin MRH domain of Glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum. J Biol Chem 288:16460–16475

    Article  CAS  PubMed  Google Scholar 

  • Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY (2000) The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 10:815–827

    Article  CAS  PubMed  Google Scholar 

  • Reitman ML, Trowbridge IS, Kornfeld S (1982) A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein-processing enzyme. J Biol Chem 257:10357–10363

    CAS  PubMed  Google Scholar 

  • Robledo-Ortiz CI, Flores-Carreon A, Hernandez-Cervantes A, Alvarez-Vargas A, Lee KK, Diaz-Jimenez DF, Munro CA, Cano-Canchola C, Mora-Montes HM (2012) Isolation and functional characterization of Sporothrix schenckii ROT2, the encoding gene for the endoplasmic reticulum glucosidase II. Fungal Biol 116:910–918

    Article  CAS  PubMed  Google Scholar 

  • Sakai K, Hirai M, Minoshima S, Kudoh J, Fukuyama R, Shimizu N (1989) Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80 K protein. Genomics 5:309–315

    Article  CAS  PubMed  Google Scholar 

  • Saunier B, Kilker RD Jr, Tkacz JS, Quaroni A, Herscovics A (1982) Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases. J Biol Chem 257:14155–14161

    CAS  PubMed  Google Scholar 

  • Saxena S, Shailubhai K, Dong-Yu B, Vijay IK (1987) Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland. Biochem J 247:563–570

    CAS  PubMed  Google Scholar 

  • Sousa M, Parodi AJ (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14:4196–4203

    CAS  PubMed  Google Scholar 

  • Sousa MC, Ferrero-Garcia MA, Parodi AJ (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: glycoprotein glucosyltransferase. Biochemistry 31:97–105

    Article  CAS  PubMed  Google Scholar 

  • Stigliano ID, Alculumbre SG, Labriola CA, Parodi AJ, D’Alessio C (2011) Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo. Mol Biol Cell 22:1810–1823

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Strous GJ, Van Kerkhof P, Brok R, Roth J, Brada D (1987) Glucosidase II, a protein of the endoplasmic reticulum with high mannose oligosaccharide chains and a rapid turnover. J Biol Chem 262:3620–3625

    CAS  PubMed  Google Scholar 

  • Treml K, Meimaroglou D, Hentges A, Bause E (2000) The a- and b-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver. Glycobiology 10:493–502

    Article  CAS  PubMed  Google Scholar 

  • Trombetta ES, Simons JF, Helenius A (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem 271:27509–27516

    Article  CAS  PubMed  Google Scholar 

  • Ugalde RA, Staneloni RJ, Leloir LF (1980) Microsomal glucosidases of rat liver. Partial purification and inhibition by disaccharides. Eur J Biochem 113:97–103

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Road, Athens, GA, 30602, USA

    Alison V. Nairn & Prof. Kelley W. Moremen

Authors
  1. Alison V. Nairn
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Prof. Kelley W. Moremen
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Alison V. Nairn .

Editor information

Editors and Affiliations

  1. RIKEN-Max-Planck Joint Research Center for Systems Chemical Biology, RIKEN, Wako, Saitama, Japan

    Naoyuki Taniguchi

  2. Department of Biochemistry, Kochi University, Medical School, Nankoku, Kochi, Japan

    Koichi Honke

  3. Sanford Burnham Medical Research Institute, La Jolla, California, USA

    Minoru Fukuda

  4. Research Center for Medical Glycoscience (RCMG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan

    Hisashi Narimatsu

  5. RIKEN-Max-Planck Joint Research Center for Systems Chemical Biology, RIKEN, Wako, Saitama, Japan

    Yoshiki Yamaguchi

  6. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan

    Takashi Angata

Rights and permissions

Reprints and permissions

Copyright information

© 2014 Springer Japan

About this entry

Cite this entry

Nairn, A.V., Moremen, K.W. (2014). Glucosidase, Alpha Neutral AB; Glucosidase II Subunit Beta (GANAB, PRKCSH, α-Glucosidase II). In: Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (eds) Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54240-7_140

Download citation

Publish with us

Policies and ethics

Search

Navigation