Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding‐defective glycoproteins
2007; Wiley; Volume: 581; Issue: 19 Linguagem: Inglês
10.1016/j.febslet.2007.04.070
ISSN1873-3468
AutoresSilvia Olivari, Maurizio Molinari,
Tópico(s)Trypanosoma species research and implications
ResumoProteins 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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