| pubmed-article:20065073 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20065073 | lifeskim:mentions | umls-concept:C1253959 | lld:lifeskim |
| pubmed-article:20065073 | lifeskim:mentions | umls-concept:C0024742 | lld:lifeskim |
| pubmed-article:20065073 | lifeskim:mentions | umls-concept:C1425927 | lld:lifeskim |
| pubmed-article:20065073 | lifeskim:mentions | umls-concept:C1879647 | lld:lifeskim |
| pubmed-article:20065073 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:20065073 | pubmed:dateCreated | 2010-4-8 | lld:pubmed |
| pubmed-article:20065073 | pubmed:abstractText | Glycoprotein folding and degradation in the endoplasmic reticulum (ER) is mediated by the ER quality control system. Mannose trimming plays an important role by forming specific N-glycans that permit the recognition and sorting of terminally misfolded conformers for ERAD (ER-associated degradation). The EDEM (ER degradation enhancing alpha-mannosidase-like protein) subgroup of proteins belonging to the Class I alpha1,2-mannosidase family (glycosylhydrolase family 47) has been shown to enhance ERAD. We recently reported that overexpression of EDEM3 enhances glycoprotein ERAD with a concomitant increase in mannose-trimming activity in vivo. Herein, we report that overexpression of EDEM1 produces Glc(1)Man(8)GlcNAc(2) isomer C on terminally misfolded null Hong Kong alpha1-antitrypsin (NHK) in vivo. Levels of this isomer increased throughout the chase period and comprised approximately 10% of the [(3)H]mannose-labeled N-glycans on NHK after a 3-h chase. Furthermore, overexpression of EDEM1 E220Q containing a mutation in a conserved catalytic residue essential for alpha1,2-mannosidase activity did not yield detectable levels of Glc(1)Man(8)GlcNAc(2) isomer C. Yet, the same extent of NHK ERAD-enhancement was observed in both EDEM1 and EDEM1 E220Q overexpressing cells. This can be attributed to both wild-type and mutant EDEM1 inhibiting aberrant NHK dimer formation. We further analyzed the N-glycan profile of total cellular glycoproteins from HepG2 cells stably overexpressing EDEM1 and found that the relative amount of Man(7)GlcNAc(2) isomer A, which lacks the terminal B and C branch mannoses, was increased compared to parental HepG2 cells. Based on this observation, we conclude that EDEM1 activity trims mannose from the C branch of N-glycans in vivo. | lld:pubmed |
| pubmed-article:20065073 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20065073 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20065073 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20065073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20065073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20065073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20065073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20065073 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20065073 | pubmed:month | May | lld:pubmed |
| pubmed-article:20065073 | pubmed:issn | 1460-2423 | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:HerscovicsAnn... | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:NagataKazuhir... | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:KatoKoichiK | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:WadaIkuoI | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:TremblayLinda... | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:HosokawaNobuk... | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:SlenoBarryB | lld:pubmed |
| pubmed-article:20065073 | pubmed:author | pubmed-author:KamiyaYukikoY | lld:pubmed |
| pubmed-article:20065073 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20065073 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:20065073 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20065073 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20065073 | pubmed:pagination | 567-75 | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:meshHeading | pubmed-meshheading:20065073... | lld:pubmed |
| pubmed-article:20065073 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20065073 | pubmed:articleTitle | EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans. | lld:pubmed |
| pubmed-article:20065073 | pubmed:affiliation | Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8397, Japan. nobukoh@frontier.kyoto-u.ac.jp | lld:pubmed |
| pubmed-article:20065073 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20065073 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:9695 | entrezgene:pubmed | pubmed-article:20065073 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20065073 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20065073 | lld:pubmed |
