Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9

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• 作者：Jürgen Roth ; Christian Zuber
• 关键词：Protein N ; glycosylation ; Endoplasmic reticulum ; Glucosidase I ; Glucosidase II ; Glucosyltransferase ; ER mannosidase I ; EDEM1 ; OS ; 9 ; Protein folding ; ERAD
• 刊名：Histochemistry and Cell Biology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：147
• 期：2
• 页码：269-284
• 全文大小：
• 刊物类别：Medicine
• 刊物主题：Biomedicine, general; Cell Biology; Biochemistry, general; Developmental Biology;
• 出版者：Springer Berlin Heidelberg
• ISSN：1432-119X
• 卷排序：147

文摘

Protein N-glycosylation and quality control of protein folding as well as the connected ER-associated degradation of misfolded glycoproteins (ERAD) are not only evolutionary highly conserved but also functionally linked. It is now established that particular N-glycan structures which result from processing reactions by exo-glycosidases in the ER are of importance for glycoprotein folding and for ERAD. Thus, mono-glucosylated N-glycan intermediates harbor structural information which is important for promoting glycoprotein folding. On the other hand, specific mannose-trimmed N-glycans harbor structural information for routing misfolded glycoproteins to ERAD. In this review, we summarize current knowledge concerning the role played by glucosidases I and II, in concert with the bifunctional glucosyltransferase and calnexin/calreticulin in glycoprotein folding, the role of conventional ER mannosidase I in concert with the mannosidase EDEM1 in handling and routing of misfolded glycoproteins, and how the bifunctional OS-9 provides a link to the ER dislocon for degradation.