Protein quality control in the early secretory pathway

被引：506

作者：

Anelli, Tiziana ^{[1
]}

Sitia, Roberto ^{[1
]}

机构：

[1] Univ Vita Salute, Ist Sci San Raffaele, DiBiT HSR, Dept Funct Genom & Mol Biol, I-20132 Milan, Italy

来源：

EMBO JOURNAL | 2008年 / 27卷 / 02期

关键词：

endoplasmic reticulum; ER signalling; folding; protein degradation; protein secretion;

D O I：

10.1038/sj.emboj.7601974

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：

Eukaryotic cells are able to discriminate between native and non-native polypeptides, selectively transporting the former to their final destinations. Secretory proteins are scrutinized at the endoplasmic reticulum ( ER)-Golgi interface. Recent findings reveal novel features of the underlying molecular mechanisms, with several chaperone networks cooperating in assisting the maturation of complex proteins and being selectively induced to match changing synthetic demands. 'Public' and 'private' chaperones, some of which enriched in specializes subregions, operate for most or selected substrates, respectively. Moreover, sequential checkpoints are distributed along the early secretory pathway, allowing efficiency and fidelity in protein secretion.

引用

页码：315 / 327

页数：13

共 177 条

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