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Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding‐defective glycoproteins
Author(s) -
Olivari Silvia,
Molinari Maurizio
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.04.070
Subject(s) - calnexin , endoplasmic reticulum , chaperone (clinical) , protein folding , glycoprotein , endoplasmic reticulum associated protein degradation , folding (dsp implementation) , chemistry , glycan , microbiology and biotechnology , unfolded protein response , biochemistry , biology , calreticulin , medicine , electrical engineering , pathology , engineering
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.