Skip Navigation



Glycobiology Advance Access published online on November 10, 2004
Glycobiology, doi:10.1093/glycob/cwi014
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow Correction to PDF
Right arrow All Versions of this Article:
15/4/421    most recent
cwi014v1
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 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 arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Mast, S. W.
Right arrow Articles by Moremen, K. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mast, S. W.
Right arrow Articles by Moremen, K. W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Received October 27, 2004
Accepted November 5, 2004

ORIGINAL ARTICLES

Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins

Steven W. Mast 1, Krista Diekman 2, Khanita Karaveg 1, Ann Davis 1, Richard N. Sifers 2, and Kelley W. Moremen 1*

1 Department of Biochemistry and Molecular Biology and Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602-4712
2 Department of Pathology, Baylor College of Medicine, Houston, TX 77030-3498; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030-3498

* To whom correspondence should be addressed.
Kelley W. Moremen, E-mail: moremen{at}uga.edu


  Abstract

In the endoplasmic reticulum (ER), misfolded proteins are retro-translocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins, but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we have characterized one of the EDEM homologs from H. sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no {alpha}-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded {alpha}1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded {alpha}1-antitrypsin indicating that the protein is involved in ERAD.

Keywords: EDEM; EDEM2; ERAD; ER quality control; mannosidase.
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
 J. Biol. Chem.Home page
N. Hosokawa, I. Wada, K. Nagasawa, T. Moriyama, K. Okawa, and K. Nagata
Human XTP3-B Forms an Endoplasmic Reticulum Quality Control Scaffold with the HRD1-SEL1L Ubiquitin Ligase Complex and BiP
J. Biol. Chem., July 25, 2008; 283(30): 20914 - 20924.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
M. Dong, J. P. Bridges, K. Apsley, Y. Xu, and T. E. Weaver
ERdj4 and ERdj5 Are Required for Endoplasmic Reticulum-associated Protein Degradation of Misfolded Surfactant Protein C
Mol. Biol. Cell, June 1, 2008; 19(6): 2620 - 2630.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. J. Caramelo and A. J. Parodi
Getting In and Out from Calnexin/Calreticulin Cycles
J. Biol. Chem., April 18, 2008; 283(16): 10221 - 10225.
[Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
E. Avezov, Z. Frenkel, M. Ehrlich, A. Herscovics, and G. Z. Lederkremer
Endoplasmic Reticulum (ER) Mannosidase I Is Compartmentalized and Required for N-Glycan Trimming to Man5 6GlcNAc2 in Glycoprotein ER-associated Degradation
Mol. Biol. Cell, January 1, 2008; 19(1): 216 - 225.
[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
 GlycobiologyHome page
K. Kato and Y. Kamiya
Structural views of glycoprotein-fate determination in cells
Glycobiology, October 1, 2007; 17(10): 1031 - 1044.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. Banerjee, P. Vishwanath, J. Cui, D. J. Kelleher, R. Gilmore, P. W. Robbins, and J. Samuelson
The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation
PNAS, July 10, 2007; 104(28): 11676 - 11681.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
C. Zuber, J. H. Cormier, B. Guhl, R. Santimaria, D. N. Hebert, and J. Roth
EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
PNAS, March 13, 2007; 104(11): 4407 - 4412.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
N. Kawasaki, I. Matsuo, K. Totani, D. Nawa, N. Suzuki, D. Yamaguchi, N. Matsumoto, Y. Ito, and K. Yamamoto
Detection of Weak Sugar Binding Activity of VIP36 using VIP36-streptavidin Complex and Membrane-based Sugar Chains
J. Biochem., February 1, 2007; 141(2): 221 - 229.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
L. W. Ruddock and M. Molinari
N-glycan processing in ER quality control
J. Cell Sci., November 1, 2006; 119(21): 4373 - 4380.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
B. Mueller, B. N. Lilley, and H. L. Ploegh
SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
J. Cell Biol., October 23, 2006; 175(2): 261 - 270.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Hirao, Y. Natsuka, T. Tamura, I. Wada, D. Morito, S. Natsuka, P. Romero, B. Sleno, L. O. Tremblay, A. Herscovics, et al.
EDEM3, a Soluble EDEM Homolog, Enhances Glycoprotein Endoplasmic Reticulum-associated Degradation and Mannose Trimming
J. Biol. Chem., April 7, 2006; 281(14): 9650 - 9658.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
B. Di Jeso, Y.-n. Park, L. Ulianich, A. S. Treglia, M. L. Urbanas, S. High, and P. Arvan
Mixed-Disulfide Folding Intermediates between Thyroglobulin and Endoplasmic Reticulum Resident Oxidoreductases ERp57 and Protein Disulfide Isomerase
Mol. Cell. Biol., November 15, 2005; 25(22): 9793 - 9805.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
F. Movsichoff, O. A. Castro, and A. J. Parodi
Characterization of Schizosaccharomyces pombe ER {alpha}-Mannosidase: A Reevaluation of the Role of the Enzyme on ER-associated Degradation
Mol. Biol. Cell, October 1, 2005; 16(10): 4714 - 4724.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Karaveg and K. W. Moremen
Energetics of Substrate Binding and Catalysis by Class 1 (Glycosylhydrolase Family 47) {alpha}-Mannosidases Involved in N-Glycan Processing and Endoplasmic Reticulum Quality Control
J. Biol. Chem., August 19, 2005; 280(33): 29837 - 29848.
[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.