Journal
GLYCOBIOLOGY
Volume 15, Issue 4, Pages 421-436Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwi014
Keywords
EDEM; EDEM2; ERAD; ER quality control; mannosidase
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Funding
- NCRR NIH HHS [P41 RR005351, RR05351] Funding Source: Medline
- NHLBI NIH HHS [HL62553, R01 HL062553, R01 HL62553] Funding Source: Medline
- NIDDK NIH HHS [R01 DK064232] Funding Source: Medline
- NIGMS NIH HHS [R01 GM047533, GM47533] Funding Source: Medline
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In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated 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 characterize one of the EDEM homologs from Homo 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.
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