Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum

被引：566

作者：

Michalak, Marek ^{[1
]}

Groenendyk, Jody ^{[1
]}

Szabo, Eva ^{[2
]}

Gold, Leslie I. ^{[3
,4
]}

Opas, Michal ^{[2
]}

机构：

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

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

[3] NYU, Sch Med, Dept Med, New York, NY 10016 USA

[4] NYU, Sch Med, Dept Pathol, New York, NY 10016 USA

来源：

BIOCHEMICAL JOURNAL | 2009年 / 417卷

基金：

加拿大健康研究院;

关键词：

calcium homoeostasis; calreticulin; endoplasmic reticulum (ER); protein folding; quality control; CELL-SURFACE CALRETICULIN; CLASS-I MOLECULES; BINDING PROTEIN CALRETICULIN; RECEPTOR-RELATED PROTEIN; TUMOR-SPECIFIC IMMUNITY; QUALITY-CONTROL; MUTATIONAL ANALYSIS; CA2+ CONCENTRATION; INDUCED APOPTOSIS; GENE-EXPRESSION;

D O I：

10.1042/BJ20081847

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：

Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved ill regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. The protein impacts on store-operated Ca2+ influx and influences Ca2+ dependent transcriptional pathways during embryonic development. Calreticulin is also involved in the folding of newly synthesized proteins and glycoproteins and, together with calnexin (an integral ER membrane chaperone similar to calreticulin) and ERp57 [ER protein of 57 kDa; a PDI (protein disulfide-isomerase)-like ER-resident protein], constitutes the 'calreticulin/calnexin cycle' that is responsible for folding and quality control of newly synthesized glycoproteins. In recent years, calreticulin has been implicated to play a role in many biological systems, including functions inside and outside the ER, indicating that the protein is a multi-process molecule. Regulation of Ca2+ homoeostasis and ER Ca2+ buffering by calreticulin might be the key to explain its multi-process property.

引用

页码：651 / 666

页数：16

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