Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems

被引:206
作者
Brodsky, Jeffrey L. [1 ]
Skach, William R. [2 ]
机构
[1] Univ Pittsburgh, Dept Biol Sci, Pittsburgh, PA 15260 USA
[2] Oregon Hlth & Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97231 USA
基金
美国国家卫生研究院;
关键词
ER-ASSOCIATED DEGRADATION; TRANSMEMBRANE CONDUCTANCE REGULATOR; POLYTOPIC MEMBRANE-PROTEIN; UBIQUITIN LIGASE COMPLEX; DISULFIDE BOND FORMATION; UNFOLDED-PROTEIN; MISFOLDED PROTEINS; PROTEASOMAL DEGRADATION; CRYSTAL-STRUCTURE; CARBOHYDRATE-RECOGNITION;
D O I
10.1016/j.ceb.2011.05.004
中图分类号
Q2 [细胞生物学];
学科分类号
071013 [干细胞生物学];
摘要
The evolution of eukaryotes was accompanied by an increased need for intracellular communication and cellular specialization. Thus, a more complex collection of secreted and membrane proteins had to be synthesized, modified, and folded. The endoplasmic reticulum (ER) thereby became equipped with devoted enzymes and associated factors that both catalyze the production of secreted proteins and remove damaged proteins. A means to modify ER accommodate and destroy misfolded Not surprisingly, a growing number of human diseases are linked to various facets of ER function. Each of these topics will be discussed in this article, with an emphasis on recent reports in the literature that employed diverse models.
引用
收藏
页码:464 / 475
页数:12
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