Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins |
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Authors: | Olivari Silvia Molinari Maurizio |
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Institution: | Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland. silvia.olivari@irb.unisi.ch |
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Abstract: | Proteins synthesized in the endoplasmic reticulum (ER) lumen are exposed to several dedicated chaperones and folding factors that ensure efficient maturation. Nevertheless, protein folding remains error-prone and mutations in the polypeptide sequence may significantly reduce folding-efficiency. Folding-incompetent proteins carrying N-glycans are extracted from futile folding cycles in the calnexin chaperone system upon intervention of EDEM1, EDEM2 and EDEM3, three ER-stress-induced members of the glycosyl hydrolase 47 family. This review describes current knowledge about mechanisms regulating folding and disposal of glycoproteins. |
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Keywords: | Endoplasmic reticulum Protein folding ER-associated degradation (ERAD) EDEM1 EDEM2 EDEM3 |
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