Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol

被引：52

作者：

Christis, Chantal ^{[1
]}

Lubsen, Nicolette H. ^{[2
]}

Braakman, Ineke ^{[1
]}

机构：

[1] Univ Utrecht, Bijvoet Ctr Biomol Res, Fac Sci, NL-3584 CH Utrecht, Netherlands

[2] Radboud Univ Nijmegen, NL-6525 ED Nijmegen, Netherlands

来源：

FEBS JOURNAL | 2008年 / 275卷 / 19期

基金：

英国医学研究理事会;

关键词：

chaperone; disulfide bond formation; endoplasmic reticulum; ERAD; glycosylation; lectin; oligomerization; protein folding; quality control; unfolded protein response;

D O I：

10.1111/j.1742-4658.2008.06590.x

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：

A correct three-dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimensional structure is formed. In general, plasma membrane and secreted proteins, as well as those residing in compartments along the endocytic and exocytic pathways, fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins, which renders this compartment a protein-folding factory. This review focuses on protein folding in the endoplasmic reticulum, and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol.

引用

页码：4700 / 4727

页数：28

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