Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

FEBS Letters

Lecomte, Fabienne J.L¹  Abell, Benjamin M¹  High, Stephen¹  Russell, Sarah J¹  Oliver, Jason D¹ 

[1]School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester M13 9PT, UK

关键词: Endoplasmic reticulum;    Glycoprotein;    Protein folding;    Molecular chaperone;    Calnexin;    ERp57;   

DOI  :  10.1016/S0014-5793(00)01666-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The endoplasmic reticulum (ER) is a major site of protein synthesis and its inside, or lumen, is a major site of protein folding. The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding.

【 授权许可】

Unknown