Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (56)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Jakob, C. A.
Right arrow Articles by Roth, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jakob, C. A.
Right arrow Articles by Roth, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, Vol 8, 155-164, Copyright © 1998 by Society for Glycobiology

ORIGINAL ARTICLES

Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo

CA Jakob, P Burda, S te Heesen, M Aebi and J Roth
Division of Cell and Molecular Pathology, Institute for Microbiology, Zurich, Switzerland.

In higher eukaryotes a quality control system monitoring the folding state of glycoproteins is located in the ER and is composed of the proteins calnexin, calreticulin, glucosidase II, and UDP-glucose: glycoprotein glucosyltransferase. It is believed that the innermost glucose residue of the N- linked oligosaccharide of a glycoprotein serves as a tag in this control system and therefore performs an important function in the protein folding pathway. To address this function, we constructed Saccharomyces cerevisiae strains which contain nonglucosylated (G0), monoglucosylated (G1), or diglucosylated (G2) glycoproteins in the ER and used these strains to study the role of glucose residues in the ER processing of glycoproteins. These alterations of the oligosaccharide structure did not result in a growth phenotype, but the induction of the unfolded protein response upon treatment with DTT was much higher in G0 and G2 strains as compared to wild-type and G1 strains. Our results provide in vivo evidence that the G1 oligosaccharide is an active oligosaccharide structure in the ER glycoprotein processing pathway of S.cerevisiae. Furthermore, by analyzing N- linked oligosaccharides of the constructed strains we can directly show that no general glycoprotein glucosyltransferase exists in S. cerevisiae.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
R. P Quinn, S. J Mahoney, B. M Wilkinson, D. J Thornton, and C. J Stirling
A novel role for Gtb1p in glucose trimming of N-linked glycans
Glycobiology, December 1, 2009; 19(12): 1408 - 1416.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
T. Watanabe, K. Totani, I. Matsuo, J.-i. Maruyama, K. Kitamoto, and Y. Ito
Genetic analysis of glucosidase II {beta}-subunit in trimming of high-mannose-type glycans
Glycobiology, August 1, 2009; 19(8): 834 - 840.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
S. Clerc, C. Hirsch, D. M. Oggier, P. Deprez, C. Jakob, T. Sommer, and M. Aebi
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
J. Cell Biol., January 12, 2009; 184(1): 159 - 172.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
D. N. Hebert and M. Molinari
In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
Physiol Rev, October 1, 2007; 87(4): 1377 - 1408.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. M. Wilkinson, J. Purswani, and C. J. Stirling
Yeast GTB1 Encodes a Subunit of Glucosidase II Required for Glycoprotein Processing in the Endoplasmic Reticulum
J. Biol. Chem., March 10, 2006; 281(10): 6325 - 6333.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. D'Alessio, J. J. Caramelo, and A. J. Parodi
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation
J. Biol. Chem., December 9, 2005; 280(49): 40417 - 40427.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
A. Faridmoayer and C. H. Scaman
Binding residues and catalytic domain of soluble Saccharomyces cerevisiae processing alpha-glucosidase I
Glycobiology, December 1, 2005; 15(12): 1341 - 1348.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
C. G. Frank and M. Aebi
ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis
Glycobiology, November 1, 2005; 15(11): 1156 - 1163.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. A. Wearsch, C. A. Jakob, A. Vallin, R. A. Dwek, P. M. Rudd, and P. Cresswell
Major Histocompatibility Complex Class I Molecules Expressed with Monoglucosylated N-Linked Glycans Bind Calreticulin Independently of Their Assembly Status
J. Biol. Chem., June 11, 2004; 279(24): 25112 - 25121.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. Chavan, T. Suzuki, M. Rekowicz, and W. Lennarz
Genetic, biochemical, and morphological evidence for the involvement of N-glycosylation in biosynthesis of the cell wall {beta}1,6-glucan of Saccharomyces cerevisiae
PNAS, December 23, 2003; 100(26): 15381 - 15386.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
K. Hirano, C. Zuber, J. Roth, and M. Ziak
The Proteasome Is Involved in the Degradation of Different Aquaporin-2 Mutants Causing Nephrogenic Diabetes Insipidus
Am. J. Pathol., July 1, 2003; 163(1): 111 - 120.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. D'Alessio, E. S. Trombetta, and A. J. Parodi
Nucleoside Diphosphatase and Glycosyltransferase Activities Can Localize to Different Subcellular Compartments in Schizosaccharomyces pombe
J. Biol. Chem., June 13, 2003; 278(25): 22379 - 22387.
[Abstract] [Full Text] [PDF]

Home page
 Eukaryot CellHome page
A. Miseta, M. Tokes-Fuzesi, D. P. Aiello, and D. M. Bedwell
A Saccharomyces cerevisiae Mutant Unable To Convert Glucose to Glucose-6-Phosphate Accumulates Excessive Glucose in the Endoplasmic Reticulum due to Core Oligosaccharide Trimming
Eukaryot. Cell, June 1, 2003; 2(3): 534 - 541.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
K. Hirano, M. Ziak, K. Kamoshita, Y. Sukenaga, S. Kametani, Y. Shiga, J. Roth, and H. Akanuma
N-linked oligosaccharide processing enzyme glucosidase II produces 1,5-anhydrofructose as a side product
Glycobiology, December 1, 2000; 10(12): 1283 - 1289.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
C. Zuber, M. J. Spiro, B. Guhl, R. G. Spiro, and J. Roth
Golgi Apparatus Immunolocalization of Endomannosidase Suggests Post-Endoplasmic Reticulum Glucose Trimming: Implications for Quality Control
Mol. Biol. Cell, December 1, 2000; 11(12): 4227 - 4240.
[Abstract] [Full Text]

Home page
 GlycobiologyHome page
M. F. Pelletier, A. Marcil, G. Sevigny, C. A. Jakob, D. C. Tessier, E. Chevet, R. Menard, J. J.M. Bergeron, and D. Y. Thomas
The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo
Glycobiology, August 1, 2000; 10(8): 815 - 827.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
D. C. Tessier, D. Dignard, A. Zapun, A. Radominska-Pandya, A. J. Parodi, J. J.M. Bergeron, and D. Y. Thomas
Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme
Glycobiology, April 1, 2000; 10(4): 403 - 412.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. F. Cipollo and R. B. Trimble
The Accumulation of Man6GlcNAc2-PP-dolichol in the Saccharomyces cerevisiae Delta alg9 Mutant Reveals a Regulatory Role for the Alg3p alpha 1,3-Man Middle-arm Addition in Downstream Oligosaccharide-lipid and Glycoprotein Glycan Processing
J. Biol. Chem., February 11, 2000; 275(6): 4267 - 4277.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. D'Alessio, F. Fernandez, E. S. Trombetta, and A. J. Parodi
Genetic Evidence for the Heterodimeric Structure of Glucosidase II. THE EFFECT OF DISRUPTING THE SUBUNIT-ENCODING GENES ON GLYCOPROTEIN FOLDING
J. Biol. Chem., September 3, 1999; 274(36): 25899 - 25905.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
O. Castro, L. Y. Chen, A. J. Parodi, and C. Abeijón
Uridine Diphosphate-Glucose Transport into the Endoplasmic Reticulum of Saccharomyces cerevisiae: In Vivo and In Vitro Evidence
Mol. Biol. Cell, April 1, 1999; 10(4): 1019 - 1030.
[Abstract] [Full Text]

Home page
 JCBHome page
S. Fanchiotti, F. Fernandez, C. D'Alessio, and A. J. Parodi
The UDP-Glc:Glycoprotein Glucosyltransferase Is Essential for Schizosaccharomyces pombe Viability under Conditions of Extreme Endoplasmic Reticulum Stress
J. Cell Biol., November 2, 1998; 143(3): 625 - 635.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
C. A. Jakob, P. Burda, J. Roth, and M. Aebi
Degradation of Misfolded Endoplasmic Reticulum Glycoproteins in Saccharomyces cerevisiae Is Determined by a Specific Oligosaccharide Structure
J. Cell Biol., September 7, 1998; 142(5): 1223 - 1233.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
S. Shahinian, G. J. P. Dijkgraaf, A.-M. Sdicu, D. Y. Thomas, C. A. Jakob, M. Aebi, and H. Bussey
Involvement of Protein N-Glycosyl Chain Glucosylation and Processing in the Biosynthesis of Cell Wall ss-1,6-Glucan of Saccharomyces cerevisiae
Genetics, June 1, 1998; 149(2): 843 - 856.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
C. Zuber, J.-y. Fan, B. Guhl, A. Parodi, J. H. Fessler, C. Parker, and J. Roth
Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
PNAS, September 11, 2001; 98(19): 10710 - 10715.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.