Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57

被引：127

作者：

Bedard, K ^{[1
]}

Szabo, E

Michalak, M

Opas, M

机构：

[1] Univ Alberta, Membrane Prot Res Grp, Edmonton, AB T6G 2H7, Canada

[2] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada

[3] Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON M5S 1A8, Canada

来源：

INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL 245 | 2005年 / 245卷

基金：

加拿大健康研究院;

关键词：

adhesion; calreticulin; calnexin; ERp57; protein folding; calcium homeostasis;

D O I：

10.1016/S0074-7696(05)45004-4

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Glycosylated proteins destined for the cell surface or to be secreted from the cell are trafficked through the endoplasmic reticulum during synthesis and folding. Correct folding is determined in large part by the sequence of the protein, but it is also assisted by interaction with enzymes and chaperones of the endoplasmic reticulum. Calreticulin, calnexin, and ERp57 are among the endoplasmic chaperones that interact with partially folded glycoproteins and determine if the proteins are to be released from the endoplasmic reticulum to be expressed, or alternatively, if they are to be sent to the proteosome for degradation. Studies on the effect of alterations in the expression and function of these proteins are providing information about the importance of this quality control system, as well as uncovering other important functions these proteins play outside of the endoplasmic reticulum.

引用

页码：91 / 121

页数：31

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