Glycoprotein folding in the endoplasmic reticulum

被引:13
作者
Benham, AM
Braakman, I
机构
[1] Univ Utrecht, Dept Bioorgan Chem, NL-3584 CH Utrecht, Netherlands
[2] Univ Amsterdam, Acad Med Ctr, Dept Biochem, NL-1105 AZ Amsterdam, Netherlands
关键词
protein folding; chaperones; ER; glycosylation; ERAD;
D O I
10.1080/10409230091169258
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Our understanding of eukaryotic protein folding in the endoplasmic reticulum has increased enormously over the last 5 years. In this review, we summarize some of the major research themes that have captivated researchers in this field during the last years of the 20th century. We follow the path of a typical protein as it emerges from the ribosome and enters the reticular environment. While many of these events are shared between different polypeptide chains, we highlight some of the numerous differences between proteins, between cell types, and between the chaperones utilized by different ER glycoproteins. Finally, we consider the likely advances in this field as the new century unfolds and we address the prospect of a unified understanding of how protein folding, degradation, and translation an coordinated within a cell.
引用
收藏
页码:433 / 473
页数:41
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