| http://purl.uniprot.org/citations/29784879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29784879 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein folding in the cell is regulated by several quality-control mechanisms. Correct folding of glycoproteins in the endoplasmic reticulum (ER) is tightly monitored by the recognition of glycan signals by lectins in the ER-associated degradation (ERAD) pathway. In mammals, mannose trimming from N-glycans is crucial for disposal of misfolded glycoproteins. The mannosidases responsible for this process are ER mannosidase I and ER degradation-enhancing α-mannosidase-like proteins (EDEMs). However, the molecular mechanism of mannose removal by EDEMs remains unclear, partly owing to the difficulty of reconstituting mannosidase activity in vitro Here, our analysis of EDEM3-mediated mannose-trimming activity on a misfolded glycoprotein revealed that ERp46, an ER-resident oxidoreductase, associates stably with EDEM3. This interaction, which depended on the redox activity of ERp46, involved formation of a disulfide bond between the cysteine residues of the ERp46 redox-active sites and the EDEM3 α-mannosidase domain. In a defined in vitro system consisting of recombinant proteins purified from HEK293 cells, the mannose-trimming activity of EDEM3 toward the model misfolded substrate, the glycoprotein T-cell receptor α locus (TCRα), was reconstituted only when ERp46 had established a covalent interaction with EDEM3. On the basis of these findings, we propose that disposal of misfolded glycoproteins through mannose trimming is tightly connected to redox-mediated regulation in the ER."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.ra118.003129"xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/author | "Ito S."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/author | "Yu S."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/author | "Hosokawa N."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/author | "Wada I."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/pages | "10663-10674"xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/title | "ER-resident protein 46 (ERp46) triggers the mannose-trimming activity of ER degradation-enhancing alpha-mannosidase-like protein 3 (EDEM3)."xsd:string |
| http://purl.uniprot.org/citations/29784879 | http://purl.uniprot.org/core/volume | "293"xsd:string |
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