In vitro mapping of calnexin interaction with ribosomes

被引:11
作者
Delom, F
Chevet, E [1 ]
机构
[1] McGill Univ, Dept Surg, Montreal, PQ H3A 2B2, Canada
[2] McGill Univ, Montreal Prote Network, Montreal, PQ H3A 2B2, Canada
基金
加拿大健康研究院;
关键词
endoplasmic reticulum; ribosome; translocon; calnexin; ribosomal protein L4;
D O I
10.1016/j.bbrc.2005.12.149
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
Calnexin is an endoplasmic reticulum (ER) resident type I integral membrane phosphoprotein. This protein is actively involved in the ER glycoprotein quality control through its luminal domain. In addition, although calnexin also interacts with membrane-bound ribosomes. the nature of this interaction remains poorly characterized. Herein, using in vitro approaches, we demonstrate that calnexin cytosolic domain directly interacts with, at least 5 ribosomal proteins. Furthermore, we characterize more specifically its interaction with the ribosomal protein L4 and that L4 binds to the 19 carboxy terminal amino acids of calnexin. We suggest that the direct interaction of calnexin with membrane-bound ribosomes may represent a regulatory mechanism for its lectin-like chaperone function. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:39 / 44
页数:6
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